5z7r

Crystal structure of crotonase from Clostridium acetobutylicum

spinqualitylabelsall models 5z7r, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5z7r is a 3 chain structure with sequence from Cloab. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: crt, CA_C2712 (CLOAB) Activity: Short-chain-enoyl-CoA hydratase, with EC number 4.2.1.150 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CRT_CLOAB] Catalyzes the reversible hydration of crotonyl-CoA. Can also use hexenoyl-CoA but not higher analogs. Publication Abstract from PubMed Crotonase from Clostridium acetobutylicum (CaCRT) is an enzyme that catalyzes the dehydration of 3-hydroxybutyryl-CoA to crotonyl-CoA in the n-butanol biosynthetic pathway. To investigate the molecular mechanism underlying n-butanol biosynthesis, we determined the crystal structures of the CaCRT protein in apo- and acetoacetyl-CoA bound forms. Similar to other canonical crotonase enzymes, CaCRT forms a hexamer by the dimerization of two trimers. A crystal structure of CaCRT in complex with acetoacetyl-CoA revealed that Ser69 and Ala24 to be signature residues of CaCRT, which results in a distinct ADP binding mode wherein the ADP moiety is bound at a different position compared with other crotonases. We also revealed that the substrate specificity of crotonase enzymes is determined by both the structural feature of the alpha3 helix region and the residues contributing the enoyl-CoA binding pocket. A tight formed alpha3 helix and two phenylalanine residues, Phe143 and Phe233, aid CaCRT to accommodate crotonyl-CoA as the substrate. The key residues involved in substrate binding, enzyme catalysis and substrate specificity were confirmed by site-directed mutagenesis. Structural insights into substrate specificity of crotonase from the n-butanol producing bacterium Clostridium acetobutylicum.,Kim EJ, Kim YJ, Kim KJ Biochem Biophys Res Commun. 2014 Aug 29;451(3):431-5. doi:, 10.1016/j.bbrc.2014.07.139. Epub 2014 Aug 7. PMID:25110148 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Enoyl-CoA hydratase 3D structures

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