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Structure paper

TitleEngineering a Highly Efficient Carboligase for Synthetic One-Carbon Metabolism.
Journal, issue, pagesAcs Catalysis, Vol. 11, Page 5396-5404, Year 2021
Publish dateNov 12, 2020 (structure data deposition date)
AuthorsNattermann, M. / Burgener, S. / Pfister, P. / Chou, A. / Schulz, L. / Lee, S.H. / Paczia, N. / Zarzycki, J. / Gonzalez, R. / Erb, T.J.
External linksAcs Catalysis / PubMed:34484855
MethodsX-ray diffraction
Resolution1.9 - 2.8 Å
Structure data

PDB-7ayg:
oxalyl-CoA decarboxylase from Methylorubrum extorquens with bound TPP and ADP
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-7b2e:
quadruple mutant of oxalyl-CoA decarboxylase from Methylorubrum extorquens with bound TPP and ADP
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-TPP:
THIAMINE DIPHOSPHATE

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • methylorubrum extorquens am1 (bacteria)
  • methylorubrum extorquens (strain atcc 14718 / dsm 1338 / jcm 2805 / ncimb 9133 / am1) (bacteria)
KeywordsLYASE / Decarboxylase / Carboxylase / Ligase / Formyl-CoA / Oxalyl-CoA / Mandelyl-CoA

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