Journal Issue - Volume 10 Issue 12 (December 2001)
Crystal structure of calcium‐free human sorcin: A member of the penta‐EF‐hand protein family
- Xiaoling Xie, Maureen D. Dwyer, Lora Swenson, Matthew H. Parker, Martyn C. Botfield
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.36701 (p 2419-2425)
Abstract Sorcin is a 22 kD calcium‐binding protein that is found in a wide variety of cell types, such as heart, muscle, brain and adrenal medulla. It belongs to the penta‐EF‐hand (PEF) protein family, which contains five EF‐hand motifs that associate with membranes in a calcium‐dependent manner. Prototypic members of this family are the calcium‐binding domains of calpain, such as calpain dVI. Full‐length human sorcin has been...
Structure and dynamics of translation initiation factor aIF‐1A from the archaeon Methanococcus jannaschii determined by NMR spectroscopy
- Wei Li, David W. Hoffman
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.18201 (p 2426-2438)
Abstract Translation initiation factor 1A (aIF‐1A) from the archaeon Methanococcus jannaschii was expressed in Escherichia coli, purified, and characterized in terms of its structure and dynamics using multidimensional NMR methods. The protein was found to be a member of the OB‐fold family of RNA‐associated proteins, containing a barrel of five beta‐strands, a feature that is shared with the homologous eukaryotic translation initiation factor...
Analysis of crystal structures of aspartic proteinases: On the role of amino acid residues adjacent to the catalytic site of pepsin‐like enzymes
- Natalia S. Andreeva, Lev D. Rumsh
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.25801 (p 2439-2450)
Abstract To elucidate the role of amino acid residues adjacent to the catalytic site of pepsin‐like enzymes, we analyzed and compared the crystal structures of these enzymes, their complexes with inhibitors, and zymogens in the active site area (a total of 82 structures). In addition to the water molecule (W1) located between the active carboxyls and playing a role of the nucleophile during catalytic reaction, another water molecule...
Effects of charged amino‐acid mutation on the solution structure of cytochrome c
- Chengmin Qian, Yong Yao, Keqiong Ye, Jinfeng Wang, Wenxia Tang, Yunhua Wang, Wenhu Wang, Junxia Lu, Yi Xie, Zhongxian Huang
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.12401 (p 2451-2459)
Abstract The solution structure of oxidized bovine microsomal cytochrome b5 mutant (E48, E56/A, D60/A) has been determined through 1524 meaningful nuclear Overhauser effect constraints together with 190 pseudocontact shift constraints. The final family of 35 conformers has rmsd values with respect to the mean structure of 0.045±0.009 nm and 0.088±0.011 nm for backbone and heavy atoms, respectively. A characteristic of this mutant is that of ...
Motif‐based fold assignment
- Łukasz Salwiński, David Eisenberg
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.14401 (p 2460-2469)
Abstract Conventional fold recognition techniques rely mainly on the analysis of the entire sequence of a protein. We present an MBA method to improve performance of any conventional sequence‐based fold assignment. The method uses sequence motifs, such as those defined in the Prosite database, and the SwissProt annotation of the fold library. When combined with a simple SDP method, the coverage of MBA is comparable to the results...
Structure determination of human and murine β‐defensins reveals structural conservation in the absence of significant sequence similarity
- Finn Bauer, Kristian Schweimer, Enno Klüver, Jose‐Ramon Conejo‐Garcia, Wolf‐Georg Forssmann, Paul Rösch, Knut Adermann, Heinrich Sticht
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.24401 (p 2470-2479)
Abstract Defensins are cationic and cysteine‐rich peptides that play a crucial role in the host defense against microorganisms of many organisms by their capability to permeabilize bacterial membranes. The low sequence similarity among the members of the large mammalian β‐defensin family suggests that their antimicrobial activity is largely independent of their primary structure. To investigate to what extent these defensins share a...
Free energies of protein decoys provide insight into determinants of protein stability
- Yury N. Vorobjev, Jan Hermans
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.15501 (p 2498-2506)
Abstract We have calculated the stability of decoy structures of several proteins (from the CASP3 models and the Park and Levitt decoy set) relative to the native structures. The calculations were performed with the force field–consistent ES/IS method, in which an implicit solvent (IS) model is used to calculate the average solvation free energy for snapshots from explicit simulations (ESs). The conformational free energy is...
Substitution rates in α‐helical transmembrane proteins
- Timothy J. Stevens, Isaiah T. Arkin
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.10501 (p 2507-2517)
Abstract It has been shown previously that some membrane proteins have a conserved core of amino acid residues. This idea not only serves to orient helices during model building exercises but may also provide insight into the structural role of residues mediating helix–helix interactions. Using experimentally determined high‐resolution structures of α‐helical transmembrane proteins we show that, of the residues within the...
Characterization of the structure and dynamics of amyloidogenic variants of human lysozyme by NMR spectroscopy
- Aaron K. Chamberlain, Veronique Receveur, Andrew Spencer, Christina Redfield, Christopher M. Dobson
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.28101 (p 2525-2530)
Abstract The structures and dynamics of the native states of two mutational variants of human lysozyme, I56T and D67H, both associated with non‐neuropathic systemic amyloidosis, have been investigated by NMR spectroscopy. The 1H and 15N main‐chain amide chemical shifts of the I56T variant are very similar to those of the wild‐type protein, but those of the D67H variant are greatly altered for 28 residues in the β‐domain. This finding is...
pH‐induced folding of an apoptotic coiled coil
- Kaushik Dutta, Andrei Alexandrov, He Huang, Steven M. Pascal
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.28801 (p 2531-2540)
Abstract Par‐4 is a 38‐kD protein pivotal to the apoptotic pathways of various cell types, most notably prostate cells and neurons, where it has been linked to prostate cancer and various neurodegenerative disorders including Alzheimer's and Huntington's diseases and HIV encephalitis. The C‐terminal region of Par‐4 is responsible for homodimerization and the ability of Par‐4 to interact with proposed effector molecules. In this...
Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N‐terminal domain
- Fabrizio Chiti, Monica Bucciantini, Cristina Capanni, Niccolò Taddei, Christopher M. Dobson, Massimo Stefani
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.10201 (p 2541-2547)
Abstract The HypF N‐terminal domain has been found to convert readily from its native globular conformation into protein aggregates with the characteristics of amyloid fibrils associated with a variety of human diseases. This conversion was achieved by incubation at acidic pH or in the presence of moderate concentrations of trifluoroethanol. Electron microscopy showed that the fibrils grown in the presence of trifluoroethanol were...
Identification of residues critical for metallo‐β‐lactamase function by codon randomization and selection
- Isabel C. Materon, Timothy Palzkill
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.40884 (p 2556-2565)
Abstract IMP‐1 β‐lactamase is a zinc metallo‐enzyme encoded by the transferable blaIMP‐1 gene, which confers resistance to virtually all β‐lactam antibiotics including carbapenems. To understand how IMP‐1 recognizes and hydrolyzes β‐lactam antibiotics it is important to determine which amino acid residues are critical for catalysis and which residues control substrate specificity. We randomized 27 individual codons in the blaIMP‐1 gene to...
Catalytic and binding poly‐reactivities shared by two unrelated proteins: The potential role of promiscuity in enzyme evolution
- Leo C. James, Dan S. Tawfik
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.14601 (p 2600-2607)
Abstract It is generally accepted that enzymes evolved via gene duplication of existing proteins. But duplicated genes can serve as a starting point for the evolution of a new function only if the protein they encode happens to exhibit some activity towards this new function. Although the importance of such catalytic promiscuity in enzyme evolution has been proposed, little is actually known regarding how common promiscuous...
The C‐terminal domain of biotin protein ligase from E. coli is required for catalytic activity
- Anne Chapman‐Smith, Terrence D. Mulhern, Fiona Whelan, John E. Cronan, John C. Wallace
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.22401 (p 2608-2617)
Abstract Biotin protein ligase of Escherichia coli, the BirA protein, catalyses the covalent attachment of the biotin prosthetic group to a specific lysine of the biotin carboxyl carrier protein (BCCP) subunit of acetyl‐CoA carboxylase. BirA also functions to repress the biotin biosynthetic operon and synthesizes its own corepressor, biotinyl‐5′‐AMP, the catalytic intermediate in the biotinylation reaction. We have previously ...
Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor
- Larry H. Weaver, Keehwan Kwon, Dorothy Beckett, Brian W. Matthews
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.32701 (p 2618-2622)
Abstract A model is suggested for the complex between the biotin repressor of Escherichia coli, BirA, and BCCP, the biotin carboxyl carrier protein to which BirA transfers biotin. The model is consistent with prior physical and biochemical studies. Measurement of transfer rates for variants of BirA with single‐site mutations in the proposed BirA:BCCP interface region also provides support. The unique feature of the proposed interaction between...




