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TitleProbing the dynamic interface between trimethylamine dehydrogenase (TMADH) and electron transferring flavoprotein (ETF) in the TMADH-2ETF complex: role of the Arg-alpha237 (ETF) and Tyr-442 (TMADH) residue pair.
Journal, issue, pagesBiochemistry, Vol. 47, Page 5168-5181, Year 2008
Publish dateMar 20, 2008 (structure data deposition date)
AuthorsBurgess, S.G. / Messiha, H.L. / Katona, G. / Rigby, S.E. / Leys, D. / Scrutton, N.S.
External linksBiochemistry / PubMed:18407658
MethodsX-ray diffraction
Resolution1.65 - 2 Å
Structure data

PDB-3clr:
Crystal structure of the R236A ETF mutant from M. methylotrophus
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3cls:
Crystal structure of the R236C mutant of ETF from Methylophilus methylotrophus
Method: X-RAY DIFFRACTION / Resolution: 1.65 Å

PDB-3clt:
Crystal structure of the R236E mutant of Methylophilus methylotrophus ETF
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-3clu:
Crystal structure of the R236K mutant from Methylophilus methylotrophus ETF
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-PO4:
PHOSPHATE ION

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

ChemComp-HOH:
WATER

Source
  • methylophilus methylotrophus (bacteria)
KeywordsELECTRON TRANSPORT / ETF / TMADH / electron transfer / flavoprotein / FAD / Transport / dynamic interface

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