1dtn
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MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE
OverviewOverview
In the high-resolution X-ray structure of mandelate racemase (MR) with the, competitive inhibitor (S)-atrolactate bound in the active site [Landro, J., A., Gerlt, J. A., Kozarich, J. W., Koo, C. W., Shah, V. J., Kenyon, G. L., Neidhart, D. J., Fujita, J., & Petsko, G. A. (1994) Biochemistry 33, 635-643], the carboxylic acid group of Glu 317 is hydrogen-bonded to the, carboxylate group of the bound inhibitor. This geometry suggests that the, carboxylic acid functional group of Glu 317 participates as a general acid, catalyst in the concerted general acid-general base catalyzed formation of, a stabilized enolic tautomer of mandelic acid as a reaction intermediate., To test this hypothesis, the E317Q mutant of MR was constructed and, subjected to high-resolution X-ray structural analysis ... [(full description)]
About this StructureAbout this Structure
1DTN is a [Single protein] structure of sequence from [Pseudomonas aeruginosa] with MG and APG as [ligands]. Active as [[1]], with EC number [5.1.2.2]. Full crystallographic information is available from [OCA].
ReferenceReference
Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317., Mitra B, Kallarakal AT, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL, Biochemistry. 1995 Mar 7;34(9):2777-87. PMID:7893689
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