2XED

Nocardia farcinica maleate cis-trans isomerase C194S mutant with a covalently bound succinylcysteine intermediate

Summary for 2XED

Entry DOI	10.2210/pdb2xed/pdb
Related	2XEC
Descriptor	PUTATIVE MALEATE ISOMERASE, SUCCINIC ACID (3 entities in total)
Functional Keywords	isomerase, nicotinic acid catabolism, cofactor-independent cis-trans isomerase
Biological source	NOCARDIA FARCINICA
Total number of polymer chains	4
Total formula weight	115780.25
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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.95 Å)

Structure validation