3KXP
Crystal Structure of E-2-(Acetamidomethylene)succinate Hydrolase
Summary for 3KXP
| Entry DOI | 10.2210/pdb3kxp/pdb |
| Descriptor | Alpha-(N-acetylaminomethylene)succinic acid hydrolase, CHLORIDE ION (3 entities in total) |
| Functional Keywords | alpha/beta hydrolase, plp degradation, e-2-(acetamidomethylene)succinate, hydrolase |
| Biological source | Mesorhizobium loti |
| Total number of polymer chains | 12 |
| Total formula weight | 410282.02 |
| Authors | McCulloch, K.M.,Mukherjee, T.,Begley, T.P.,Ealick, S.E. (deposition date: 2009-12-03, release date: 2010-02-09, Last modification date: 2024-10-09) |
| Primary citation | McCulloch, K.M.,Mukherjee, T.,Begley, T.P.,Ealick, S.E. Structure determination and characterization of the vitamin B(6) degradative enzyme (E)-2-(acetamidomethylene)succinate hydrolase. Biochemistry, 49:1226-1235, 2010 Cited by PubMed Abstract: The gene identification and kinetic characterization of (E)-2-(acetamidomethylene)succinate (E-2AMS) hydrolase has recently been described. This enzyme catalyzes the final reaction in the degradation of vitamin B(6) and produces succinic semialdehyde, acetate, ammonia, and carbon dioxide from E-2AMS. The structure of E-2AMS hydrolase was determined to 2.3 A using SAD phasing. E-2AMS hydrolase is a member of the alpha/beta hydrolase superfamily and utilizes a serine/histidine/aspartic acid catalytic triad. Mutation of either the nucleophilic serine or the aspartate resulted in inactive enzyme. Mutation of an additional serine residue in the active site causes the enzyme to be unstable and is likely structurally important. The structure also provides insight into the mechanism of hydrolysis of E-2AMS and identifies several potential catalytically important residues. PubMed: 20099871DOI: 10.1021/bi901812p PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.26 Å) |
Structure validation
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