2B7L

Crystal Structure of CTP:Glycerol-3-Phosphate Cytidylyltransferase from Staphylococcus aureus

2B7L の概要

• エントリーDOI: 10.2210/pdb2b7l/pdb
• 関連するPDBエントリー: 1COZ 1N1D
• 分子名称: glycerol-3-phosphate cytidylyltransferase (1 entity in total)
• 機能のキーワード: cytidylyltransferase, rossmann fold, transferase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63372.52

構造登録者

Fong, D.H.,Yim, V.C.-N.,D'Elia, M.A.,Brown, E.D.,Berghuis, A.M. (登録日: 2005-10-04, 公開日: 2006-06-27, 最終更新日: 2023-08-23)

主引用文献

Fong, D.H.,Yim, V.C.-N.,D'Elia, M.A.,Brown, E.D.,Berghuis, A.M.
Crystal structure of CTP:glycerol-3-phosphate cytidylyltransferase from Staphylococcus aureus: examination of structural basis for kinetic mechanism.
Biochim.Biophys.Acta, 1764:63-69, 2006

PubMed Abstract: Integrity of the cell wall is essential for bacterial survival, and as a consequence components involved in its biosynthesis can potentially be exploited as targets for antibiotics. One such potential target is CTP:glycerol-3-phosphate cytidylyltransferase. This enzyme (TarD(Sa) in Staphylococcus aureus and TagD(Bs) in Bacillus subtilis) catalyzes the formation of CDP-glycerol, which is used for the assembly of linkages between peptidoglycan and teichoic acid polymer in Gram-positive bacteria. Intriguingly, despite the high sequence identity between TarD(Sa) and TagD(Bs) (69% identity), kinetic studies show that these two enzymes differ markedly in their kinetic mechanism and activity. To examine the basis for the disparate enzymological properties, we have determined the crystal structure of TarD(Sa) in the apo state to 3 A resolution, and performed equilibrium sedimentation analysis. Comparison of the structure with that of CTP- and CDP-glycerol-bound TagD(Bs) crystal structures reveals that the overall structure of TarD(Sa) is essentially the same as that of TagD(Bs), except in the C-terminus, where it forms a helix in TagD(Bs) but is disordered in the apo TarD(Sa) structure. In addition, TarD(Sa) can exist both as a tetramer and as a dimer, unlike TagD(Bs), which is a dimer. These observations shed light on the structural basis for the differing kinetic characteristics between TarD(Sa) and TagD(Bs).

PubMed: 16344011
DOI: 10.1016/j.bbapap.2005.10.015

実験手法

X-RAY DIFFRACTION (3 Å)