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Structure paper

TitleStructural basis of the action of pulvomycin and GE2270 A on elongation factor Tu.
Journal, issue, pagesBiochemistry, Vol. 45, Page 6846-6857, Year 2006
Publish dateNov 18, 2005 (structure data deposition date)
AuthorsParmeggiani, A. / Krab, I.M. / Okamura, S. / Nielsen, R.C. / Nyborg, J. / Nissen, P.
External linksBiochemistry / PubMed:16734421
MethodsX-ray diffraction
Resolution1.4 - 1.6 Å
Structure data

PDB-2c77:
EF-Tu complexed with a GTP analog and the antibiotic GE2270 A
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-2c78:
EF-Tu complexed with a GTP analog and the antibiotic pulvomycin
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

Chemicals

ChemComp-GNP:
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / GppNHp, GMPPNP, energy-carrying molecule analogue*YM

ChemComp-MG:
Unknown entry

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

ChemComp-PUL:
(1S,2S,3E,5E,7E,10S,11S,12S)-12-[(2R,4E,6E,8Z,10R,12E,14E,16Z,18S,19Z)-10,18-DIHYDROXY-12,16,19-TRIMETHYL-11,22-DIOXOOX

Source
  • thermus thermophilus (bacteria)
  • planobispora rosea (bacteria)
KeywordsHYDROLASE/ANTIBIOTIC / HYDROLASE-ANTIBIOTIC COMPLEX / THIOPEPTIDE / ANTIBIOTIC / ANTIBACTERIAL / THIAZOLE / OXAZOLE / HYDROLASE / GTPASE / TRANSLATION ELONGATION FACTOR / PROTEIN SYNTHESIS / NUCLEOTIDE-BINDING / PHOSPHORYLATION / GTP-BINDING / PROTEIN BIOSYNTHESIS / ELONGATION FACTOR

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