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Structure paper

TitleIdentification of an SH3-Binding Motif in a New Class of Methionine Aminopeptidases from Mycobacterium tuberculosis Suggests a Mode of Interaction with the Ribosome
Journal, issue, pagesBiochemistry, Vol. 44, Page 7166-7174, Year 2005
Publish dateNov 18, 2004 (structure data deposition date)
AuthorsAddlagatta, A. / Quillin, M.L. / Omotoso, O. / Liu, J.O. / Matthews, B.W.
External linksBiochemistry / PubMed:15882055
MethodsX-ray diffraction
Resolution1.51 - 1.6 Å
Structure data

PDB-1y1n:
Identification of SH3 motif in M. Tuberculosis methionine aminopeptidase suggests a mode of interaction with the ribosome
Method: X-RAY DIFFRACTION / Resolution: 1.51 Å

PDB-1yj3:
Crystal structure analysis of product bound methionine aminopeptidase Type 1c from Mycobacterium Tuberculosis
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-CO:
Unknown entry

ChemComp-MET:
METHIONINE

ChemComp-BME:
BETA-MERCAPTOETHANOL

Source
  • mycobacterium tuberculosis (bacteria)
KeywordsHYDROLASE / Methionine aminopeptidase; MtMetAP1B; PxxP; SH3; ribosome; L24 / pita bread fold / complexed with Two Cobalt and Methionine / C285 modification by oxidized beta-mercapto ethanol

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