Journal Issue - Volume 18 Issue 3 (March 2009)
In This Issue
- Published in Wiley Interscience on Feb 23, 2009
- DOI: 10.1002/pro.74 (p v)
No abstract.
Knitting and untying the protein network: Modulation of protein ensembles as a therapeutic strategy
- Susana Gordo, Ernest Giralt
- Published in Wiley Interscience on Dec 29, 2008
- DOI: 10.1002/pro.43 (p 481-493)
Proteins constitute the working machinery and structural support of all organisms. In performing a given function, they must adopt highly specific structures that can change with their level of activity, often through the direct or indirect action of other proteins. Indeed, proteins typically function within an ensemble, rather than individually. Hence, they must be sufficiently flexible to interact with each other and execute diverse tasks. The discovery that errors within these groups can...
A review about nothing: Are apolar cavities in proteins really empty?
- Brian W. Matthews, Lijun Liu
- Published in Wiley Interscience on Jan 12, 2009
- DOI: 10.1002/pro.61 (p 494-502)
Cavities within proteins that are strictly apolar typically appear to be empty. It has been suggested, however, that water molecules may be present within such cavities but are too disordered to be seen in conventional crystallographic analyses. In contrast, it is argued here that solvent mobility will be limited by the size of the cavity and for this reason high-occupancy solvent in cavities of typical volume should be readily detectable using X-ray crystallography. Recent experimental studies...
Structural evidence suggests that antiactivator ExsD from Pseudomonas aeruginosa is a DNA binding protein
- Robert C. Bernhards, Xing Jing, Nancy J. Vogelaar, Howard Robinson, Florian D. Schubot
- Published in Wiley Interscience on Jan 06, 2009
- DOI: 10.1002/pro.48 (p 503-513)
The opportunistic pathogen P. aeruginosa utilizes a type III secretion system (T3SS) to support acute infections in predisposed individuals. In this bacterium, expression of all T3SS-related genes is dependent on the AraC-type transcriptional activator ExsA. Before host contact, the T3SS is inactive and ExsA is repressed by the antiactivator protein ExsD. The repression, thought to occur through direct interactions between the two proteins, is relieved upon opening of the type III secretion...
Biochemical characterization, localization, and tissue distribution of the longer form of mouse SIRT3
- Lei Jin, Heidi Galonek, Kristine Israelian, Wendy Choy, Michael Morrison, Yu Xia, Xiaohong Wang, Yihua Xu, Yuecheng Yang, Jesse J. Smith, Ethan Hoffmann, David P. Carney, Robert B. Perni, Michael R. Jirousek, Jean E. Bemis, Jill C. Milne, David A. Sinclair, Christoph H. Westphal
- Published in Wiley Interscience on Jan 06, 2009
- DOI: 10.1002/pro.50 (p 514-525)
SIRT3 is a key mitochondrial protein deacetylase proposed to play key roles in regulating mitochondrial metabolism but there has been considerable debate about its actual size, the sequences required for activity, and its subcellular localization. A previously cloned mouse SIRT3 has high sequence similarity with the C-terminus of human SIRT3 but lacks an N-terminal mitochondrial targeting sequence and has no detectable deacetylation activity in vitro. Using 5 rapid amplification of cDNA ends,...
The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state
- Sung Lun Lin, Arash Zarrine-Afsar, Alan R. Davidson
- Published in Wiley Interscience on Jan 06, 2009
- DOI: 10.1002/pro.52 (p 526-536)
Trimethylamine-N-oxide (TMAO) is a naturally occurring osmolyte that stabilizes proteins against denaturation. Although the impact of TMAO on the folding thermodynamics of many proteins has been well characterized, far fewer studies have investigated its effects on protein folding kinetics. In particular, no previous studies have used -value analysis to determine whether TMAO may alter the structure of the folding transition state. Here we have measured the effects on folding kinetics of 16...
Structural plasticity of the phage P22 tail needle gp26 probed with xenon gas
- Adam S. Olia, Sherwood Casjens, Gino Cingolani
- Published in Wiley Interscience on Jan 11, 2009
- DOI: 10.1002/pro.53 (p 537-548)
The tail needle, gp26, is a highly stable homo-trimeric fiber found in the tail apparatus of bacteriophage P22. In the mature virion, gp26 is responsible for plugging the DNA exit channel, and likely plays an important role in penetrating the host cell envelope. In this article, we have determined the 1.98 Å resolution crystal structure of gp26 bound to xenon gas. The structure led us to identify a calcium and a chloride ion intimately bound at the interior of -helical core, as well as seven...
Involvement of a carboxylated lysine in UV damage endonuclease
- Elisabeth M. Meulenbroek, Keti Paspaleva, Ellen A. J. Thomassen, Jan Pieter Abrahams, Nora Goosen, Navraj S. Pannu
- Published in Wiley Interscience on Jan 06, 2009
- DOI: 10.1002/pro.54 (p 549-558)
UV damage endonuclease is a DNA repair enzyme that can both recognize damage such as UV lesions and introduce a nick directly 5 to them. Recently, the crystal structure of the enzyme from Thermus thermophilus was solved. In the electron density map of this structure, unexplained density near the active site was observed at the tip of Lys229. Based on this finding, it was proposed that Lys229 is post-translationally modified. In this article, we give evidence that this modification is a carboxyl...
Cupryphans, metal-binding, redox-active, redesigned conopeptides
- Marco Barba, Anatoli P. Sobolev, Cristina Romeo, M. Eugenia Schininà, Donatella Pietraforte, Luisa Mannina, Giovanni Musci, Fabio Polticelli
- Published in Wiley Interscience on Jan 09, 2009
- DOI: 10.1002/pro.58 (p 559-568)
Contryphans are bioactive peptides, isolated from the venom of marine snails of the genus Conus, which are characterized by the short length of the polypeptide chain and the high degree of unusual post-translational modifications. The cyclization of the polypeptide chain through a single disulphide bond, the presence of two conserved Pro residues, and the epimerization of a Trp/Leu residue confer to Contryphans a stable and well-defined structure in solution, conserved in all members of the...
Triad of polar residues implicated in pH specificity of acidic mammalian chitinase
- Andrea M. Olland, James Strand, Eleonora Presman, Robert Czerwinski, Diane Joseph-McCarthy, Rustem Krykbaev, Gerhard Schlingmann, Rajiv Chopra, Laura Lin, Margaret Fleming, Ron Kriz, Mark Stahl, William Somers, Lori Fitz, Lidia Mosyak
- Published in Wiley Interscience on Jan 11, 2009
- DOI: 10.1002/pro.63 (p 569-578)
Acidic mammalian chitinase (AMCase) is a mammalian chitinase that has been implicated in allergic asthma. One of only two active mammalian chinases, AMCase, is distinguished from other chitinases by several unique features. Here, we present the novel structure of the AMCase catalytic domain, both in the apo form and in complex with the inhibitor methylallosamidin, determined to high resolution by X-ray crystallography. These results provide a structural basis for understanding some of the...
Protease inhibitors derived from elafin and SLPI and engineered to have enhanced specificity towards neutrophil serine proteases
- Marie-Louise Zani, Kévin Baranger, Nicolas Guyot, Sandrine Dallet-Choisy, Thierry Moreau
- Published in Wiley Interscience on Jan 12, 2009
- DOI: 10.1002/pro.64 (p 579-594)
The secretory leukocyte protease inhibitor (SLPI), elafin, and its biologically active precursor trappin-2 are endogeneous low-molecular weight inhibitors of the chelonianin family that control the enzymatic activity of neutrophil serine proteases (NSPs) like elastase, proteinase 3, and cathepsin G. These inhibitors may be of therapeutic value, since unregulated NSP activities are linked to inflammatory lung diseases. However SLPI inhibits elastase and cathepsin G but not proteinase 3, while...
Lone pair ··· π interactions between water oxygens and aromatic residues: Quantum chemical studies based on high-resolution protein structures and model compounds
- Alok Jain, Venkatnarayan Ramanathan, Ramasubbu Sankararamakrishnan
- Published in Wiley Interscience on Jan 11, 2009
- DOI: 10.1002/pro.67 (p 595-605)
The electron cloud of aromatic centers is known to be involved in several noncovalent interactions such as CH···, OH···, and ··· interactions in biomolecules. Lone-pair (lp) ··· interactions have gained attention recently and their role in biomolecular structures is being recognized. In this article, we have carried out systematic analysis of high-resolution protein structures and identified more than 400 examples in which water oxygen atoms are in close contact (distance interactions...
Structure and function of Pseudomonas aeruginosa protein PA1324 (21-170)
- Kelly A. Mercier, John R. Cort, Michael A. Kennedy, Erin E. Lockert, Shuisong Ni, Matthew D. Shortridge, Robert Powers
- Published in Wiley Interscience on Jan 11, 2009
- DOI: 10.1002/pro.62 (p 606-618)
Pseudomonas aeruginosa is the prototypical biofilm-forming gram-negative opportunistic human pathogen. P. aeruginosa is causatively associated with nosocomial infections and with cystic fibrosis. Antibiotic resistance in some strains adds to the inherent difficulties that result from biofilm formation when treating P. aeruginosa infections. Transcriptional profiling studies suggest widespread changes in the proteome during quorum sensing and biofilm development. Many of the proteins found to be...
Camelid nanobodies raised against an integral membrane enzyme, nitric oxide reductase
- Katja Conrath, Alice S. Pereira, Carlos E. Martins, Cristina G. Timóteo, Pedro Tavares, Silvia Spinelli, Joerg Kinne, Christophe Flaudrops, Christian Cambillau, Serge Muyldermans, Isabel Moura, Jose J. G. Moura, Mariella Tegoni, Aline Desmyter
- Published in Wiley Interscience on Jan 21, 2009
- DOI: 10.1002/pro.69 (p 619-628)
Nitric Oxide Reductase (NOR) is an integral membrane protein performing the reduction of NO to N2O. NOR is composed of two subunits: the large one (NorB) is a bundle of 12 transmembrane helices (TMH). It contains a b type heme and a binuclear iron site, which is believed to be the catalytic site, comprising a heme b and a non-hemic iron. The small subunit (NorC) harbors a cytochrome c and is attached to the membrane through a unique TMH. With the aim to perform structural and functional studies...
Dematin exhibits a natively unfolded core domain and an independently folded headpiece domain
- Lin Chen, Zhenghui G. Jiang, Anwar A. Khan, Athar H. Chishti, C. James McKnight
- Published in Wiley Interscience on Jan 11, 2009
- DOI: 10.1002/pro.59 (p 629-636)
Dematin is an actin-binding protein originally identified in the junctional complex of the erythrocyte plasma membrane, and is present in many nonerythroid cells. Dematin headpiece knockout mice display a spherical red cell phenotype and develop a compensated anemia. Dematin has two domains: a 315-residue, proline-rich core domain and a 68-residue carboxyl-terminal villin-type headpiece domain. Expression of full-length dematin in E. coli as a GST recombinant protein results in truncation...



