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4I9F

Crystal structure of glycerol phosphate phosphatase Rv1692 from Mycobacterium tuberculosis in complex with calcium

4I9F の概要
エントリーDOI10.2210/pdb4i9f/pdb
関連するPDBエントリー4I9G
分子名称Glycerol 3-phosphate phosphatase, CALCIUM ION, CHLORIDE ION, ... (4 entities in total)
機能のキーワードhaloacid dehalogenase superfamily, phosphatase, glycerol 3-phosphate binding, hydrolase
由来する生物種Mycobacterium tuberculosis
タンパク質・核酸の鎖数2
化学式量合計76315.58
構造登録者
Biswas, T.,Larrouy-Maumus, G.,de Carvalho, L.P.,Tsodikov, O.V. (登録日: 2012-12-05, 公開日: 2013-07-10, 最終更新日: 2023-09-20)
主引用文献Larrouy-Maumus, G.,Biswas, T.,Hunt, D.M.,Kelly, G.,Tsodikov, O.V.,de Carvalho, L.P.
Discovery of a glycerol 3-phosphate phosphatase reveals glycerophospholipid polar head recycling in Mycobacterium tuberculosis.
Proc.Natl.Acad.Sci.USA, 110:11320-11325, 2013
Cited by
PubMed Abstract: Functional assignment of enzymes encoded by the Mycobacterium tuberculosis genome is largely incomplete despite recent advances in genomics and bioinformatics. Here, we applied an activity-based metabolomic profiling method to assign function to a unique phosphatase, Rv1692. In contrast to its annotation as a nucleotide phosphatase, metabolomic profiling and kinetic characterization indicate that Rv1692 is a D,L-glycerol 3-phosphate phosphatase. Crystal structures of Rv1692 reveal a unique architecture, a fusion of a predicted haloacid dehalogenase fold with a previously unidentified GCN5-related N-acetyltransferase region. Although not directly involved in acetyl transfer, or regulation of enzymatic activity in vitro, this GCN5-related N-acetyltransferase region is critical for the solubility of the phosphatase. Structural and biochemical analysis shows that the active site features are adapted for recognition of small polyol phosphates, and not nucleotide substrates. Functional assignment and metabolomic studies of M. tuberculosis lacking rv1692 demonstrate that Rv1692 is the final enzyme involved in glycerophospholipid recycling/catabolism, a pathway not previously described in M. tuberculosis.
PubMed: 23801751
DOI: 10.1073/pnas.1221597110
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.21 Å)
構造検証レポート
Validation report summary of 4i9f
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2026-04-15に公開中

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