3vz3

Structural insights into substrate and cofactor selection by sp2771

spinqualitylabelsall models 3vz3, resolution 1.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vz3 is a 2 chain structure with sequence from Synechococcus sp. PCC 7002. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.69Å Ligands: NAP, SSN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B1XMM6_SYNP2 Publication Abstract from PubMed Aldehyde dehydrogenase (ALDH) catalyzes the oxidation of aldehydes to carboxylic acids. Cyanobacterium Synechococcus contains one ALDH enzyme (Sp2771), together with a novel 2-oxoglutarate decarboxylase, to complete a non-canonical tricarboxylic acid cycle. However, the molecular mechanisms for substrate selection and cofactor preference by Sp2771 are largely unknown. Here, we report crystal structures of wild type Sp2771, Sp2771 S419A mutant and ternary structure of Sp2771 C262A mutant in complex with NADP(+) and SSA, as well as binary structure of Gluconobacter oxydans aldehyde dehydrogenase (Gox0499) in complex with PEG. Structural comparison of Sp2771 with Gox0499, coupled with mutational analysis, demonstrates that Ser157 residue in Sp2771 and corresponding Pro159 residue in Gox0499 play critical structural roles in determining NADP(+) and NAD(+) preference for Sp2771 and Gox0499, respectively, whereas size and distribution of hydrophobic residues along the substrate binding funnel determine substrate selection. Hence, our work has provided insightful structural information into cofactor and substrate selection by ALDH. Structural basis for cofactor and substrate selection by cyanobacterium succinic semialdehyde dehydrogenase.,Yuan Z, Yin B, Wei D, Yuan YR J Struct Biol. 2013 May;182(2):125-35. doi: 10.1016/j.jsb.2013.03.001. Epub 2013 , Mar 13. PMID:23500184 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Succinate-semialdehyde dehydrogenase

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