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4Q7C

Structure of AF2299, a CDP-alcohol phosphotransferase

4Q7C の概要
エントリーDOI10.2210/pdb4q7c/pdb
関連するPDBエントリー4O6M 4O6N
分子名称AF2299, a CDP-alcohol phosphotransferase, CALCIUM ION, [(Z)-octadec-9-enyl] (2R)-2,3-bis(oxidanyl)propanoate, ... (5 entities in total)
機能のキーワードcdp-alcohol phosphotransferase, membrane protein, structural genomics, psi-biology, new york consortium on membrane protein structure, nycomps, transferase
由来する生物種Archaeoglobus fulgidus
タンパク質・核酸の鎖数2
化学式量合計88788.81
構造登録者
主引用文献Sciara, G.,Clarke, O.B.,Tomasek, D.,Kloss, B.,Tabuso, S.,Byfield, R.,Cohn, R.,Banerjee, S.,Rajashankar, K.R.,Slavkovic, V.,Graziano, J.H.,Shapiro, L.,Mancia, F.
Structural basis for catalysis in a CDP-alcohol phosphotransferase.
Nat Commun, 5:4068-4068, 2014
Cited by
PubMed Abstract: The CDP-alcohol phosphotransferase (CDP-AP) family of integral membrane enzymes catalyses the transfer of a substituted phosphate group from a CDP-linked donor to an alcohol acceptor. This is an essential reaction for phospholipid biosynthesis across all kingdoms of life, and it is catalysed solely by CDP-APs. Here we report the 2.0 Å resolution crystal structure of a representative CDP-AP from Archaeoglobus fulgidus. The enzyme (AF2299) is a homodimer, with each protomer consisting of six transmembrane helices and an N-terminal cytosolic domain. A polar cavity within the membrane accommodates the active site, lined with the residues from an absolutely conserved CDP-AP signature motif (D(1)xxD(2)G(1)xxAR...G(2)xxxD(3)xxxD(4)). Structures in the apo, CMP-bound, CDP-bound and CDP-glycerol-bound states define functional roles for each of these eight conserved residues and allow us to propose a sequential, base-catalysed mechanism universal for CDP-APs, in which the fourth aspartate (D4) acts as the catalytic base.
PubMed: 24923293
DOI: 10.1038/ncomms5068
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.102 Å)
構造検証レポート
Validation report summary of 4q7c
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2025-10-08に公開中

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