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Structure paper

TitleThe role of the beta5-alpha11 loop in the active-site dynamics of acylated penicillin-binding protein A from Mycobacterium tuberculosis
Journal, issue, pagesJ. Mol. Biol., Vol. 418, Page 316-330, Year 2012
Publish dateNov 15, 2011 (structure data deposition date)
AuthorsFedarovich, A. / Nicholas, R.A. / Davies, C.
External linksJ. Mol. Biol. / PubMed:22365933
MethodsX-ray diffraction
Resolution2 - 2.4 Å
Structure data

PDB-3un7:
Crystal structure of PBPA from MYCOBACTERIUM TUBERCULOSIS
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3upn:
Structure of penicillin-binding protein A from M. tuberculosis: imipenem acyl-enzyme complex
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3upo:
Structure of penicillin-binding protein A from M. tuberculosis: penicillin G acyl-enzyme complex
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3upp:
Structure of penicillin-binding protein A from M. tuberculosis: ceftrixaone acyl-enzyme complex
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-IM2:
(5R)-5-[(1S,2R)-1-formyl-2-hydroxypropyl]-3-[(2-{[(E)-iminomethyl]amino}ethyl)sulfanyl]-4,5-dihydro-1H-pyrrole-2-carbox / antibiotic*YM

ChemComp-PNM:
OPEN FORM - PENICILLIN G / antibiotic*YM

ChemComp-CEF:
CEFOTAXIME, C3' cleaved, open, bound form / antibiotic*YM

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsTRANSFERASE / TRANSPEPTIDASE / penicillin-binding protein / peptidoglycan / beta-lactam / Penicillin-binding protein/Antibiotic / Penicillin-binding protein-Antibiotic complex / peptidoglycan peptide

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