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TitleThe structure of the proline utilization a proline dehydrogenase domain inactivated by N-propargylglycine provides insight into conformational changes induced by substrate binding and flavin reduction.
Journal, issue, pagesBiochemistry, Vol. 49, Page 560-569, Year 2010
Publish dateAug 28, 2009 (structure data deposition date)
AuthorsSrivastava, D. / Zhu, W. / Johnson, W.H. / Whitman, C.P. / Becker, D.F. / Tanner, J.J.
External linksBiochemistry / PubMed:19994913
MethodsX-ray diffraction
Resolution2.15 Å
Structure data

PDB-3itg:
Structure the proline utilization A proline dehydrogenase domain (PutA86-630) inactivated with N-propargylglycine
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-FDA:
DIHYDROFLAVINE-ADENINE DINUCLEOTIDE

ChemComp-HOH:
WATER

Source
  • escherichia coli k-12 (bacteria)
KeywordsOXIDOREDUCTASE / Proline utilization A / PutA / flavoenzyme / mechanism-based inactivation / DNA-binding / FAD / Flavoprotein / Multifunctional enzyme / NAD / Proline metabolism / Repressor / Transcription / Transcription regulation

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