4azk

Structural basis of L-phosphoserine binding to Bacillus alcalophilus phosphoserine aminotransferase

spinqualitylabelsall models 4azk, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4azk is a 2 chain structure with sequence from Atcc 27647. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, PLP Related: 1w23, 2bhx, 2bi1, 2bi2, 2bi3, 2bi5, 2bi9, 2bia, 2bie, 2big, 4azj Activity: Phosphoserine transaminase, with EC number 2.6.1.52 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SERC_BACAO] Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. Publication Abstract from PubMed Phosphoserine aminotransferase is a vitamin B6-dependent enzyme that catalyzes the reversible conversion of 3-phosphohydroxypyruvate to L-phosphoserine using glutamate as an amine donor. In an effort to gain insight into the substrate-recognition mechanism of the enzyme, crystal structures of Bacillus alcalophilus phosphoserine aminotransferase in the presence or absence of L-phosphoserine were determined to resolutions of 1.5 and 1.6 A, respectively. Local conformational changes induced upon substrate binding were identified. However, in contrast to other aminotransferases, no domain or subunit movements were observed. Two Arg residues (Arg42 and Arg328) and two His residues (His41 and His327) were found to form a tight binding site for the phosphate group of L-phosphoserine. Comparison with Escherichia coli phosphoserine aminotransferase in complex with the substrate analogue alpha-methylglutamate revealed more extensive structural changes in the case of L-phosphoserine binding. Based on the structural analysis, the flexibility of Arg328 is proposed to be critical for substrate recognition. Structural basis of L-phosphoserine binding to Bacillus alcalophilus phosphoserine aminotransferase.,Battula P, Dubnovitsky AP, Papageorgiou AC Acta Crystallogr D Biol Crystallogr. 2013 May;69(Pt 5):804-11. doi:, 10.1107/S0907444913002096. Epub 2013 Apr 11. PMID:23633589 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphoserine aminotransferase

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