Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape

Proteins: Structure, Function and Genetics

Volumn 68, Issue 2, 2007, Pages 438-445

  Xu, Ling ^a   Sedelnikova, Svetlana E ^a   Baker, Patrick J ^a   Hunt, Alison ^b   Errington, Jeff ^c   Rice, David W ^a  

^a UNIVERSITY OF SHEFFIELD   (United Kingdom)

^b ABERDEEN ROYAL INFIRMARY   (United Kingdom)

^c NEWCASTLE UNIVERSITY   (United Kingdom)

Author keywords

Antibiotics; Cell shape; Coiled coil; Crystal structure; Essential gene; Leucine zipper; YlaN

Indexed keywords

ANTIBIOTIC AGENT; BACTERIAL PROTEIN; LEUCINE; PROTEIN SUBUNIT; PROTEIN YLAN; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS SUBTILIS; CATALYSIS; CELL SHAPE; CELL SURVIVAL; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FAMILY; PROTEIN FUNCTION; SEQUENCE ANALYSIS; STAPHYLOCOCCUS AUREUS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BACTERIA; BACTERIAL PHYSIOLOGY; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; LEUCINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; SEQUENCE HOMOLOGY, AMINO ACID; STAPHYLOCOCCUS AUREUS; XYLOSE;

STAPHYLOCOCCUS AUREUS;

EID: 34250849031     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21377     Document Type: Article

References (32)

1. Levy SB. The challenge of antibiotic resistance. Sci Am 1998; 278:46-53.
2. Kobayashi K, Ehrlich SD, Albertini A, Amati G, Andersen KK, Arnaud M, Asai K, Ashikaga S, Aymerich S, Bessieres P, Boland F, Brignell SC, Bron S, Bunai K, Chapuis J, Christiansen LC, Danchin A, Debarbouille M, Dervyn E, Deuerling E, Devine K, Devine SK, Dreesen O, Errington J, Fillinger S, Foster SJ, Fujita Y, Galizzi A, Gardan R, Eschevins C, Fukushima T, Haga K, Harwood CR, Hecker M, Hosoya D, Hullo MF, Kakeshita H, Karamata D, Kasahara Y, Kawamura F, Koga K, Koski P, Kuwana R, Imamura D, Ishimaru M, Ishikawa S, Ishio I, Le Coq D, Masson A, Mauel C, Meima R, Mellado RP, Moir A, Moriya S, Nagakawa E, Nanamiya H, Nakai S, Nygaard P, Ogura M, Ohanan T, O'Reilly M, O'Rourke M, Pragai Z, Pooley HM, Rapoport G, Rawlins JP, Rivas LA, Rivolta C, Sadaie A, Sadaie Y, Sarvas M, Sato T, Saxild HH, Scanlan E, Schumann W, Seegers J, Sekiguchi J, Sekowska A, Seror SJ, Simon M, Stragier P, Studer R, Takamatsu H, Tanaka T, Takeuchi M, Thomaides HB, Vagner V, van Dijl JM, Watabe K, Wipat A, Yamamoto H, Yamamoto M, Yamamoto Y, Yamane K, Yata K, Yoshida K, Yoshikawa H, Zuber U, Ogasawara N. Essential Bacillus subtilis genes. Proc Nat Acad Sci USA 2003;100:4678-4683.
3. Xu L, Sedelnikova SE, Baker PJ, Rice DW. Cloning, purification and preliminary crystallographic analysis of a conserved hypothetical protein, SA0961 (YlaN), from Staphylococcus aureus. Acta Crystallogr F-Struct Biol Cryst Commun 2006;62:778-780.
4. Wang LS, Trawick JD, Yamamoto R, Zamudio C. Genome-wide operon prediction in Staphylococcus aureus. Nucleic Acids Res 2004;32:3689-3702.
5. Hunt A, Rawlins JP, Thomaides HB, Errington J. Functional analysis of 11 putative essential genes in Bacillus subtilis. Microbiology 2006;152(Part 10):2895-2907.
6. Formstone A, Errington J. A magnesium-dependent mreB null mutant: implications for the role of mreB in Bacillus subtilis. Mol Microbiol 2005;55:1646-1657.
7. Leaver M, Errington J. Roles for MreC and MreD proteins in helical growth of the cylindrical cell wall in Bacillus subtilis. Mol Microbiol 2005;57:1196-1209.
8. Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680.
9. Gouet P, Courcelle E, Stuart DI, Metoz F. ESPript: analysis of multiple sequence alignments in PostScript. Bioinformatics 1999;15:305-308.
10. Schneider TR, Sheldrick GM. Substructure solution with SHELXD. Acta Crystallogr D Biol Crystallogr 2002;58:1772-1779.
11. Pape T, Schneider TR. HKL2MAP: a graphical user interface for macromolecular phasing with SHELX programs. J Appl Crystallogr 2004;37:843-844.
12. Terwilliger TC, Berendzen J. Evaluation of macromolecular electron-density map quality using the correlation of local r.m.s. density. Acta Crystallogr D Biol Crystallogr 1999;55: 1872-1877.
13. Bricogne G, Vonrhein C, Flensburg C, Schiltz M, Paciorek W. Generation, representation and flow of phase information in structure determination: recent developments in and around SHARP 2.0. Acta Crystallogr D Biol Crystallogr 2003;59:2023-2030.
14. Cowtan K. 'DM': An automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsl Protein Crystallogr 1994;31:34-38.
15. Roussel A, Cambillau C. TURBO-FRODO manual. Marseille, France: AFMB-CNRS; 1996.
16. Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004;60:2126-2132.
17. Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997;53:240-255.
18. Bailey S. The Ccp4 Suite - programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 1994;50:760-763.
19. Lee B, Richards FM. Interpretation of protein structures-estimation of static accessibility. J Mol Biol 1971;55:379-400.
20. DeLano WL. The PyMOL molecular graphics system. San Carkis, CA: DeLano Scientific; 2002.
21. Chothia C, Levitt M, Richardson D. Helix to helix packing in proteins. J Mol Biol 1981;145:215-250.
22. Jones S, Thornton JM. Protein-protein interactions - a review of protein dimer structures. Prog Biophys Mol Biol 1995;63:31-65.
23. Nicholls A, Sharp KA, Honig B. Protein folding and association - insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 1991;11:281-296.
24. Holm L, Sander C. Protein-structure comparison by alignment of distance matrices. J Mol Biol 1993;233:123-138.
25. Kim KK, Min K, Suh SW. Crystal structure of the ribosome recycling factor from Escherichia coli. Embo J 2000;19:2362-2370.
26. Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 2001;291:1553-1557.
27. Oshea EK, Rutkowski R, Kim PS. Evidence That the leucine zipper is a coiled coil. Science 1989;243:538-542.
28. Harbury PB, Zhang T, Kim PS, Alber T. A switch between 2-stranded, 3-stranded and 4-stranded coiled coils in gcn4 leucine-zipper mutants. Science 1993;262:1401-1407.
29. Porter CT, Bartlett GJ, Thornton JM. The catalytic site atlas: a resource of catalytic sites and residues identified in enzymes using structural data. Nucleic Acids Res 2004;32:D129-D133.
30. Kleywegt GJ. Recognition of spatial motifs in protein structures. J Mol Biol 1999;285:1887-1897.
31. Barker JJ. Antibacterial drug discovery and structure-based design. Drug Discov Today 2006;11:391-404.
32. Lewis LM, Engle LJ, Pierceall WE, Hughes DE, Shaw KJ. Affinity capillary electrophoresis for the screening of novel antimicrobial targets. J Biomol Screen 2004;9:303-308.