4h51 | pdb_00004h51

Crystal structure of a putative Aspartate Aminotransferase from Leishmania major Friedlin

spinqualitylabelsall models 4h51, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4h51 is a 2 chain structure with sequence from Leishmania major strain Friedlin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: EDO, LLP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4FX34_LEIMA Publication Abstract from PubMed The structures of three aspartate aminotransferases (AATs) from eukaryotic pathogens were solved within the Seattle Structural Genomics Center for Infectious Disease (SSGCID). Both the open and closed conformations of AAT were observed. Pyridoxal phosphate was bound to the active site via a Schiff base to a conserved lysine. An active-site mutant showed that Trypanosoma brucei AAT still binds pyridoxal phosphate even in the absence of the tethering lysine. The structures highlight the challenges for the structure-based design of inhibitors targeting the active site, while showing options for inhibitor design targeting the N-terminal arm. Structures of aspartate aminotransferases from Trypanosoma brucei, Leishmania major and Giardia lamblia.,Abendroth J, Choi R, Wall A, Clifton MC, Lukacs CM, Staker BL, Van Voorhis W, Myler P, Lorimer DD, Edwards TE Acta Crystallogr F Struct Biol Commun. 2015 May;71(Pt 5):566-71. doi:, 10.1107/S2053230X15001831. Epub 2015 Apr 21. PMID:25945710 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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