Structural highlights
Function
[MDH_ECOLI] Catalyzes the reversible oxidation of malate to oxaloacetate.[HAMAP-Rule:MF_01516]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 A resolution. The crystals belonged to space group C2, with unit-cell parameters a = 146.0, b = 52.0, c = 168.9 A, beta = 102.2 degrees. The structure was determined with the molecular-replacement pipeline program BALBES and was refined to a final R factor of 18.6% (R(free) = 21.4%). The final model has two dimers in the asymmetric unit. In each dimer one monomer contains the active-site loop in the open conformation, whereas in the opposing monomer the active-site loop is disordered.
Structure of Escherichia coli malate dehydrogenase at 1.45 A resolution.,Zaitseva J, Meneely KM, Lamb AL Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt, 9):866-9. Epub 2009 Aug 20. PMID:19724119[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zaitseva J, Meneely KM, Lamb AL. Structure of Escherichia coli malate dehydrogenase at 1.45 A resolution. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt, 9):866-9. Epub 2009 Aug 20. PMID:19724119 doi:10.1107/S1744309109032217
