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4EWP

Crystal structure of FabH from Micrococcus luteus

4EWP の概要
エントリーDOI10.2210/pdb4ewp/pdb
関連するPDBエントリー2EBD
分子名称3-oxoacyl-[acyl-carrier-protein] synthase 3 (2 entities in total)
機能のキーワードsynthase, transferase
由来する生物種Micrococcus luteus NCTC 2665
細胞内の位置Cytoplasm (By similarity): C5CAR9
タンパク質・核酸の鎖数6
化学式量合計220700.35
構造登録者
Pereira, J.H.,Goh, E.-B.,Keasling, J.D.,Beller, H.R.,Adams, P.D. (登録日: 2012-04-27, 公開日: 2012-10-03, 最終更新日: 2024-02-28)
主引用文献Pereira, J.H.,Goh, E.B.,Keasling, J.D.,Beller, H.R.,Adams, P.D.
Structure of FabH and factors affecting the distribution of branched fatty acids in Micrococcus luteus.
Acta Crystallogr.,Sect.D, 68:1320-1328, 2012
Cited by
PubMed Abstract: Micrococcus luteus is a Gram-positive bacterium that produces iso- and anteiso-branched alkenes by the head-to-head condensation of fatty-acid thioesters [coenzyme A (CoA) or acyl carrier protein (ACP)]; this activity is of interest for the production of advanced biofuels. In an effort to better understand the control of the formation of branched fatty acids in M. luteus, the structure of FabH (MlFabH) was determined. FabH, or β-ketoacyl-ACP synthase III, catalyzes the initial step of fatty-acid biosynthesis: the condensation of malonyl-ACP with an acyl-CoA. Analysis of the MlFabH structure provides insights into its substrate selectivity with regard to length and branching of the acyl-CoA. The most structurally divergent region of FabH is the L9 loop region located at the dimer interface, which is involved in the formation of the acyl-binding channel and thus limits the substrate-channel size. The residue Phe336, which is positioned near the catalytic triad, appears to play a major role in branched-substrate selectivity. In addition to structural studies of MlFabH, transcriptional studies of M. luteus were also performed, focusing on the increase in the ratio of anteiso:iso-branched alkenes that was observed during the transition from early to late stationary phase. Gene-expression microarray analysis identified two genes involved in leucine and isoleucine metabolism that may explain this transition.
PubMed: 22993086
DOI: 10.1107/S0907444912028351
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.198 Å)
構造検証レポート
Validation report summary of 4ewp
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-13に公開中

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