4pg7 | pdb_00004pg7

Crystal structure of S. aureus Homoserine Dehydrogenase at pH7.5

spinqualitylabelsall models 4pg7, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4pg7 is a 2 chain structure with sequence from Staphylococcus aureus M1064. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, GOL, LYS, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0M3KKV6_STAAU Publication Abstract from PubMed Homoserine dehydrogenase (HSD) is an oxidoreductase in the aspartic acid pathway. This enzyme coordinates a critical branch point of the metabolic pathway that leads to the synthesis of bacterial cell-wall components such as L-lysine and m-DAP in addition to other amino acids such as L-threonine, L-methionine and L-isoleucine. Here, a structural rationale for the hydride-transfer step in the reaction mechanism of HSD is reported. The structure of Staphylococcus aureus HSD was determined at different pH conditions to understand the basis for the enhanced enzymatic activity at basic pH. An analysis of the crystal structure revealed that Lys105, which is located at the interface of the catalytic and cofactor-binding sites, could mediate the hydride-transfer step of the reaction mechanism. The role of Lys105 was subsequently confirmed by mutational analysis. Put together, these studies reveal the role of conserved water molecules and a lysine residue in hydride transfer between the substrate and the cofactor. Structural basis for the catalytic mechanism of homoserine dehydrogenase.,Navratna V, Reddy G, Gopal B Acta Crystallogr D Biol Crystallogr. 2015 May;71(Pt 5):1216-25. doi:, 10.1107/S1399004715004617. Epub 2015 Apr 30. PMID:25945586 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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