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TitleCrystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release.
Journal, issue, pagesBiochemistry, Vol. 51, Page 10099-10108, Year 2012
Publish dateSep 19, 2012 (structure data deposition date)
AuthorsLuo, M. / Arentson, B.W. / Srivastava, D. / Becker, D.F. / Tanner, J.J.
External linksBiochemistry / PubMed:23151026
MethodsX-ray diffraction
Resolution1.359 - 1.75 Å
Structure data

PDB-4h6q:
Structure of oxidized Deinococcus radiodurans proline dehydrogenase complexed with L-tetrahydrofuroic acid
Method: X-RAY DIFFRACTION / Resolution: 1.359 Å

PDB-4h6r:
Structure of reduced Deinococcus radiodurans proline dehydrogenase
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

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

ChemComp-TFB:
TETRAHYDROFURAN-2-CARBOXYLIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-FDA:
DIHYDROFLAVINE-ADENINE DINUCLEOTIDE

ChemComp-ACT:
ACETATE ION

Source
  • deinococcus radiodurans (radioresistant)
KeywordsOXIDOREDUCTASE / BETA8-ALPHA8-BARREL / FLAVOENZYME

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