Journal Issue - Volume 14 Issue 8 (August 2005)
The implications of higher (or lower) success in secondary structure prediction of chain fragments
- Chung‐Jung Tsai, Ruth Nussinov
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051581805 (p 1943-1944)
Remodeling protein complexes: Insights from the AAA+ unfoldase ClpX and Mu transposase
- Briana M. Burton, Tania A. Baker
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051417505 (p 1945-1954)
Abstract Multiprotein complexes in the cell are dynamic entities that are constantly undergoing changes in subunit composition and conformation to carry out their functions. The protein–DNA complex that promotes recombination of the bacteriophage Mu is a prime example of a complex that must undergo specific changes to carry out its function. The Clp/Hsp100 family of AAA+ ATPases plays a critical role in mediating such changes. The...
The effect of long‐range interactions on the secondary structure formation of proteins
- Daisuke Kihara
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051479505 (p 1955-1963)
Abstract The influence of long‐range residue interactions on defining secondary structure in a protein has long been discussed and is often cited as the current limitation to accurate secondary structure prediction. There are several experimental examples where a local sequence alone is not sufficient to determine its secondary structure, but a comprehensive survey on a large data set has not yet been done. Interestingly, some...
Crystal structure of the human vascular adhesion protein‐1: Unique structural features with functional implications
- Tomi T. Airenne, Yvonne Nymalm, Heidi Kidron, David J. Smith, Marjo Pihlavisto, Marko Salmi, Sirpa Jalkanen, Mark S. Johnson, Tiina A. Salminen
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051438105 (p 1964-1974)
Abstract The expression of human vascular adhesion protein‐1 (hVAP‐1) is induced at sites of inflammation where extravasation of lymphocytes from blood to the peripheral tissue occurs. We have solved the X‐ray structure of hVAP‐1, a human copper amine oxidase (CAO), which is distinguished from other CAOs in being membrane‐bound. The dimer structure reveals some intriguing features that may have fundamental roles in the adhesive and...
The intrinsically disordered C‐terminal domain of the measles virus nucleoprotein interacts with the C‐terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded
- Jean‐Marie Bourhis, Véronique Receveur‐Bréchot, Michael Oglesbee, Xinsheng Zhang, Matthew Buccellato, Hervé Darbon, Bruno Canard, Stéphanie Finet, Sonia Longhi
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051411805 (p 1975-1992)
Abstract Measles virus is a negative‐sense, single‐stranded RNA virus within theMononegavirales order,which includes several human pathogens, including rabies, Ebola, Nipah, and Hendra viruses. Themeasles virus nucleoprotein consists of a structured N‐terminal domain, and of an intrinsically disordered C‐terminal domain, NTAIL (aa 401–525), which undergoes induced folding in the presence of the C‐terminal domain (XD, aa 459–507) of the viral...
Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT
- Carina R. Büttner, Guy R. Cornelis, Dirk W. Heinz, Hartmut H. Niemann
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051474605 (p 1993-2002)
Abstract Pathogenic Yersinia species use a type III secretion (TTS) system to deliver a number of cytotoxic effector proteins directly into the mammalian host cell. To ensure effective translocation, several such effector proteins transiently bind to specific chaperones in the bacterial cytoplasm. Correspondingly, SycT is the chaperone of YopT, a cysteine protease that cleaves the membrane‐anchor of Rho‐GTPases in the host. We have...
Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton‐gated channels
- Benjamin Chagot, Pierre Escoubas, Sylvie Diochot, Cédric Bernard, Michel Lazdunski, Hervé Darbon
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051378905 (p 2003-2010)
Abstract Acid‐sensing ion channels (ASIC) are proton‐gated sodium channels that have been implicated in pain transduction associated with acidosis in inflamed or ischemic tissues. APETx2, a peptide toxin effector of ASIC3, has been purified from an extract of the sea anemone Anthopleura elegantissima. APETx2 is a 42‐amino‐acid peptide cross‐linked by three disulfide bridges. Its three‐dimensional structure, as determined by...
A scalable, GFP‐based pipeline for membrane protein overexpression screening and purification
- David Drew, Dirk‐Jan Slotboom, Giulia Friso, Torsten Reda, Pierre Genevaux, Mikaela Rapp, Nadja M. Meindl‐Beinker, Wietske Lambert, Mirjam Lerch, Daniel O. Daley, Klaas‐Jan Van Wijk, Judy Hirst, Edmund Kunji, Jan‐Willem De Gier
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051466205 (p 2011-2017)
Abstract We describe a generic, GFP‐based pipeline for membrane protein overexpression and purification in Escherichia coli. We exemplify the use of the pipeline by the identification and characterization of E. coli YedZ, a new, membrane‐integral flavocytochrome. The approach is scalable and suitable for high‐throughput applications. The GFP‐based pipeline will facilitate the characterization of the E. coli membrane proteome and serves as an important...
The E. coli NusA carboxy‐terminal domains are structurally similar and show specific RNAP‐ and λN interaction
- Anke Eisenmann, Sabine Schwarz, Stefan Prasch, Kristian Schweimer, Paul Rösch
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051372205 (p 2018-2029)
Abstract The carboxy‐terminal domain of the transcription factor Escherichia coli NusA, NusACTD, interacts with the protein N of bacteriophage λ, λN, and the carboxyl terminus of the E. coli RNA polymerase α subunit, αCTD. We solved the solution structure of the unbound NusACTD with high‐resolution nuclear magnetic resonance (NMR). Additionally, we investigated the binding sites of λN and αCTD on NusACTD using NMR titrations. The solution ...
Interdomain side‐chain interactions in human γD crystallin influencing folding and stability
- Shannon L. Flaugh, Melissa S. Kosinski‐Collins, Jonathan King
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051460505 (p 2030-2043)
Abstract Human γD crystallin (HγD‐Crys) is a two domain, β‐sheet eye lens protein that must remain soluble throughout life for lens transparency. Single amino acid substitutions of HγD‐Crys are associated with juvenile‐onset cataracts. Features of the interface between the two domains conserved among γ‐crystallins are a central six‐residue hydrophobic cluster, and two pairs of interacting residues flanking the cluster. In HγD‐Crys...
Solution structure of the ubiquitin‐like domain of human DC‐UbP from dendritic cells
- Yong‐Guang Gao, Ai‐Xin Song, Yan‐Hong Shi, Yong‐Gang Chang, Shu‐Xun Liu, Yi‐Zi Yu, Xue‐Tao Cao, Dong‐Hai Lin, Hong‐Yu Hu
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051455505 (p 2044-2050)
Abstract The previously identified dendritic cell‐derived ubiquitin‐like protein (DC‐UbP) was implicated in cellular differentiation and apoptosis. Sequence alignment suggested that it contains a ubiquitin‐like (UbL) domain in the C terminus. Here, we present the solution NMR structure and backbone dynamics of the UbL domain of DC‐UbP. The overall structure of the domain is very similar to that of Ub despite low similarity (<30%)...
Soluble domains of telomerase reverse transcriptase identified by high‐throughput screening
- Steven A. Jacobs, Elaine R. Podell, Deborah S. Wuttke, Thomas R. Cech
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051532105 (p 2051-2058)
Abstract Telomerase is a ribonucleoprotein complex responsible for extending the ends of eukaryotic chromosomes. Structural and biophysical studies of this enzyme have been limited by the inability to produce large amounts of recombinant protein. Here we perform a high‐throughput screen to map regions of the Tetrahymena thermophila TERT (Telomerase Reverse Transcriptase) protein that are overexpressed in a soluble form in Escherichia coli using...
Protein–protein interactions as a tool for site‐specific labeling of proteins
- Marcus Jäger, Xavier Michalet, Shimon Weiss
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051384705 (p 2059-2068)
Abstract Probing structures and dynamics within biomolecules using ensemble and single‐molecule fluorescence resonance energy transfer requires the conjugation of fluorophores to proteins in a site‐specific and thermodynamically nonperturbative fashion. Using single‐molecule fluorescence‐aided molecular sorting and the chymotrypsin inhibitor 2–subtilisin BPN′ complex as an example, we demonstrate that protein–protein interactions...
Design of enhanced agonists through the use of a new virtual screening method: Application to peptides that bind class I major histocompatibility complex (MHC) molecules
- Sergio Madurga, Ignasi Belda, Xavier Llorà, Ernest Giralt
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051351605 (p 2069-2079)
Abstract A new screening procedure is described that uses docking calculations to design enhanced agonist peptides that bind to major histocompatibility complex (MHC) class I receptors. The screening process proceeds via single mutations of one amino acid at the positions that directly interact with the MHC receptor. The energetic and structural effects of these mutations have been studied using fragments of the original ligand that...
Structure—function analysis of the α5 and the α13 helices of human glucokinase: Description of two novel activating mutations
- Leda Pedelini, Maria Adelaida Garcia‐Gimeno, Alberto Marina, Juan M. Gomez‐Zumaquero, Pablo Rodriguez‐Bada, Soledad López‐Enriquez, Federico C. Soriguer, Antonio L. Cuesta‐Muñoz, Pascual Sanz
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.051485205 (p 2080-2086)
Abstract It was recently described that the α5 and the α13 helices of human pancreatic glucokinase play a major role in the allosteric regulation of the enzyme. In order to understand the structural importance of these helices, we have performed site‐directed mutagenesis to generate glucokinase derivatives with altered residues. We have analyzed the kinetic parameters of these mutated forms and compared them with wild‐type and...




