3ZE4

Crystal structure of the integral membrane diacylglycerol kinase - wild-type

3ZE4 の概要

• エントリーDOI: 10.2210/pdb3ze4/pdb
• 関連するPDBエントリー: 3ZE3 3ZE5
• 分子名称: DIACYLGLYCEROL KINASE (1 entity in total)
• 機能のキーワード: transferase, lipid metabolism, in meso crystallisation, lipid cubic phase, lipidic mesophase, membrane protein, monoacylglycerol, 7.8 mag
• 由来する生物種: ESCHERICHIA COLI K-12
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 42757.88

構造登録者

Li, D.,Lyons, J.A.,Pye, V.E.,Vogeley, L.,Aragao, D.,Caffrey, M. (登録日: 2012-12-03, 公開日: 2013-05-22, 最終更新日: 2024-02-07)

主引用文献

Li, D.,Lyons, J.A.,Pye, V.E.,Vogeley, L.,Aragao, D.,Kenyon, C.P.,Shah, S.T.A.,Doherty, C.,Aherne, M.,Caffrey, M.
Crystal Structure of the Integral Membrane Diacylglycerol Kinase.
Nature, 497:521-, 2013

PubMed Abstract: Diacylglycerol kinase catalyses the ATP-dependent phosphorylation of diacylglycerol to phosphatidic acid for use in shuttling water-soluble components to membrane-derived oligosaccharide and lipopolysaccharide in the cell envelope of Gram-negative bacteria. For half a century, this 121-residue kinase has served as a model for investigating membrane protein enzymology, folding, assembly and stability. Here we present crystal structures for three functional forms of this unique and paradigmatic kinase, one of which is wild type. These reveal a homo-trimeric enzyme with three transmembrane helices and an amino-terminal amphiphilic helix per monomer. Bound lipid substrate and docked ATP identify the putative active site that is of the composite, shared site type. The crystal structures rationalize extensive biochemical and biophysical data on the enzyme. They are, however, at variance with a published solution NMR model in that domain swapping, a key feature of the solution form, is not observed in the crystal structures.

PubMed: 23676677
DOI: 10.1038/NATURE12179

実験手法

X-RAY DIFFRACTION (3.702 Å)