4wb0

Crystal structure of the broad specificity aminotransferase from Leishmania mexicana

spinqualitylabelsall models 4wb0, resolution 1.91Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wb0 is a 2 chain structure with sequence from Leime. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CAC NonStd Res: CSO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Leishmania species are early branching eukaryotic parasites that cause difficult-to-treat tissue-damaging diseases known as leishmaniases. As a hallmark of their parasitic lifestyle, Leishmaniae express a number of aminotransferases that are involved in important cellular processes and exhibit broader substrate specificity than their mammalian host's counterparts. Here, we have determined the crystal structure of the broad specificity aminotransferase from Leishmania mexicana (LmexBSAT) at 1.91A resolution. LmexBSAT is a homodimer and belongs to the alpha-branch of family-I aminotransferases. Despite the fact that the protein was crystallized in the absence of substrates and has lost the pyridoxal-5'-phosphate (PLP) cofactor during crystallization, the structure resembles the closed, ligand-bound form of related enzymes such as chicken cytosolic aspartate aminotransferase. Its broader substrate specificity seems to be rooted in increased flexibility of a substrate-binding arginine (R291) and the interactions of this residue with the N-terminus of the second chain of the dimer. Structural basis for the relaxed substrate selectivity of Leishmania mexicana broad specificity aminotransferase.,Wen J, Nowicki C, Blankenfeldt W Mol Biochem Parasitol. 2015 Aug;202(2):34-7. doi:, 10.1016/j.molbiopara.2015.09.007. Epub 2015 Oct 8. PMID:26456583 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminotransferase 3D structures

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