2XEC

Nocardia farcinica maleate cis-trans isomerase bound to TRIS

Summary for 2XEC

• Entry DOI: 10.2210/pdb2xec/pdb
• Descriptor: PUTATIVE MALEATE ISOMERASE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: isomerase
• Biological source: NOCARDIA FARCINICA
• Total number of polymer chains: 4
• Total formula weight: 115760.61

Authors

Fisch, F.,Martinez-Fleites, C.,Baudendistel, N.,Hauer, B.,Turkenburg, J.P.,Hart, S.,Bruce, N.C.,Grogan, G. (deposition date: 2010-05-13, release date: 2010-08-18, Last modification date: 2023-12-20)

Primary citation

Fisch, F.,Fleites, C.M.,Delenne, M.,Baudendistel, N.,Hauer, B.,Turkenburg, J.P.,Hart, S.,Bruce, N.C.,Grogan, G.
A Covalent Succinylcysteine-Like Intermediate in the Enzyme-Catalyzed Transformation of Maleate to Fumarate by Maleate Isomerase.
J.Am.Chem.Soc., 132:11455-, 2010

PubMed Abstract: Maleate isomerase (MI), a member of the Asp/Glu racemase superfamily, catalyzes cis-trans isomerization of the C2-C3 double bond in maleate to yield fumarate. Mutational studies, in conjunction with the structure of the C194A mutant of Nocardia farcinica MI cocrystallized with maleate, have revealed an unprecedented mode of catalysis for the superfamily in which the isomerization reaction is initiated by nucleophilic attack of cysteine at the double bond, yielding a covalent succinylcysteine-like intermediate.

PubMed: 20677745
DOI: 10.1021/JA1053576

Experimental method

X-RAY DIFFRACTION (2.2 Å)