5Z7R
Crystal structure of crotonase from Clostridium acetobutylicum
5Z7R の概要
| エントリーDOI | 10.2210/pdb5z7r/pdb |
| 分子名称 | Short-chain-enoyl-CoA hydratase (2 entities in total) |
| 機能のキーワード | short-chain enoyl-coa hydratase, lyase |
| 由来する生物種 | Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 87151.40 |
| 構造登録者 | |
| 主引用文献 | Kim, E.J.,Kim, Y.J.,Kim, K.J. Structural insights into substrate specificity of crotonase from the n-butanol producing bacterium Clostridium acetobutylicum. Biochem. Biophys. Res. Commun., 451:431-435, 2014 Cited by PubMed Abstract: 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 α3 helix region and the residues contributing the enoyl-CoA binding pocket. A tight formed α3 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. PubMed: 25110148DOI: 10.1016/j.bbrc.2014.07.139 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.2 Å) |
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