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Structure paper

TitleA conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate.
Journal, issue, pagesBiochemistry, Vol. 48, Page 951-959, Year 2009
Publish dateAug 6, 2008 (structure data deposition date)
AuthorsOstrander, E.L. / Larson, J.D. / Schuermann, J.P. / Tanner, J.J.
External linksBiochemistry / PubMed:19140736
MethodsX-ray diffraction
Resolution1.75 - 2 Å
Structure data

PDB-3e2q:
Crystal Structure Reduced PutA86-630 Mutant Y540S Complexed with trans-4-hydroxy-L-proline
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-3e2r:
Crystal Structure PutA86-630 Mutant Y540S Complexed with L-tetrahydro-2-furoic acid
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-3e2s:
Crystal Structure Reduced PutA86-630 Mutant Y540S Complexed with L-proline
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-HYP:
4-HYDROXYPROLINE

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

ChemComp-TFB:
TETRAHYDROFURAN-2-CARBOXYLIC ACID

ChemComp-CIT:
CITRIC ACID

ChemComp-PRO:
PROLINE

Source
  • escherichia coli (E. coli)
KeywordsOXIDOREDUCTASE / Proline utilization A / PutA / flavoenzyme / DNA-binding / FAD / Flavoprotein / Multifunctional enzyme / NAD / Proline metabolism / Repressor / Transcription / Transcription regulation

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