Crystal structure of elongation factor P from Pseudomonas aeruginosa at 1.75 å resolution

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 5, 2011, Pages 1688-1693

  Choi, Sarah ^a   Choe, Jungwoo ^a  

^a University of Seoul   (South Korea)

Author keywords

Conformational change; Initiation factor; Ribosome; Translation; TRNA mimic

Indexed keywords

ELONGATION FACTOR; ELONGATION FACTOR P; TRANSFER RNA; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN STRUCTURE; PSEUDOMONAS AERUGINOSA; RIBOSOME;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE ELONGATION FACTORS; PSEUDOMONAS AERUGINOSA; SEQUENCE ALIGNMENT;

PSEUDOMONAS AERUGINOSA;

EID: 79954608920     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22992     Document Type: Article

References (27)

1. Ramakrishnan V. Ribosome structure and the mechanism of translation. Cell 2002; 108: 557-572.
2. Aoki H, Adams SL, Chung DG, Yaguchi M, Chuang SE, Ganoza MC. Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis. Nucleic Acids Res 1991; 19: 6215-6220.
3. Glick BR, Ganoza MC. Identification of a soluble protein that stimulates peptide bond synthesis. Proc Natl Acad Sci USA 1975; 72: 4257-4260.
4. Kyrpides NC, Woese CR. Universally conserved translation initiation factors. Proc Natl Acad Sci USA 1998; 95: 224-228.
5. Aoki H, Dekany K, Adams SL, Ganoza MC. The gene encoding the elongation factor P protein is essential for viability and is required for protein synthesis. J Biol Chem 1997; 272: 32254-32259.
6. An G, Glick BR, Friesen JD, Ganoza MC. Identification and quantitation of elongation factor EF-P in Escherichia coli cell-free extracts. Can J Biochem 1980; 58: 1312-1314.
7. Hanawa-Suetsugu K, Sekine S, Sakai H, Hori-Takemoto C, Terada T, Unzai S, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S. Crystal structure of elongation factor P from Thermus thermophilus HB8. Proc Natl Acad Sci USA 2004; 101: 9595-9600.
8. Kim KK, Hung LW, Yokota H, Kim R, Kim SH. Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 A resolution. Proc Natl Acad Sci USA 1998; 95: 10419-10424.
9. Peat TS, Newman J, Waldo GS, Berendzen J, Terwilliger TC. Structure of translation initiation factor 5A from Pyrobaculum aerophilum at 1.75 A resolution. Structure 1998; 6: 1207-1214.
10. Yao M, Ohsawa A, Kikukawa S, Tanaka I, Kimura M. Crystal structure of hyperthermophilic archaeal initiation factor 5A: a homologue of eukaryotic initiation factor 5A (eIF-5A). J Biochem 2003; 133: 75-81.
11. Park MH, Wolff EC, Folk JE. Is hypusine essential for eukaryotic cell proliferation?. Trends Biochem Sci 1993; 18: 475-479.
12. Schnier J, Schwelberger HG, Smit-McBride Z, Kang HA, Hershey JW. Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol Cell Biol 1991; 11: 3105-3114.
13. Yanagisawa T, Sumida T, Ishii R, Takemoto C, Yokoyama S. A paralog of lysyl-tRNA synthetase aminoacylates a conserved lysine residue in translation elongation factor P. Nat Struct Mol Biol 2010; 17: 1136-1143.
14. Blaha G, Stanley RE, Steitz TA. Formation of the first peptide bond: the structure of EF-P bound to the 70S ribosome. Science 2009; 325: 966-970.
15. Allen GS, Zavialov A, Gursky R, Ehrenberg M, Frank J. The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 2005; 121: 703-712.
16. Liljas A. Biochemistry. Leaps in translational elongation. Science 2009; 326: 677-678.
17. Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 1997; 276: 307-326.
18. Terwilliger TC, Berendzen J. Automated MAD and MIR structure solution. Acta Crystallogr D Biol Crystallogr 1999; 55(Part 4): 849-861.
19. Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, Echols N, Headd JJ, Hung LW, Kapral GJ, Grosse-Kunstleve RW, McCoy AJ, Moriarty NW, Oeffner R, Read RJ, Richardson DC, Richardson JS, Terwilliger TC, Zwart PH. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 2010; 66(Part 2): 213-221.
20. Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997; 53(Part 3): 240-255.
21. Qi G, Hayward S. Database of ligand-induced domain movements in enzymes. BMC Struct Biol 2009; 9: 13.
22. Aoki H, Xu J, Emili A, Chosay JG, Golshani A, Ganoza MC. Interactions of elongation factor EF-P with the Escherichia coli ribosome. FEBS J 2008; 275: 671-681.
23. Saini P, Eyler DE, Green R, Dever TE. Hypusine-containing protein eIF5A promotes translation elongation. Nature 2009; 459: 118-121.
24. Selmer M, Dunham CM, Murphy FVt, Weixlbaumer A, Petry S, Kelley AC, Weir JR, Ramakrishnan V. Structure of the 70S ribosome complexed with mRNA and tRNA. Science 2006; 313: 1935-1942.
25. Nakamura Y, Ito K. Making sense of mimic in translation termination. Trends Biochem Sci 2003; 28: 99-105.
26. Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M. Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1. Mol Cell 2001; 8: 1375-1382.
27. Lancaster L, Kiel MC, Kaji A, Noller HF. Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing. Cell 2002; 111: 129-140.