4TV5

Crystal Structure of Citrate Synthase SbnG

4TV5 の概要

• エントリーDOI: 10.2210/pdb4tv5/pdb
• 関連するPDBエントリー: 4TV6
• 分子名称: 2-dehydro-3-deoxyglucarate aldolase, CALCIUM ION (3 entities in total)
• 機能のキーワード: siderophore biosynthesis, iron, citrate synthase, lyase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28835.05

構造登録者

Kobylarz, M.J.,Grigg, J.C.,Murphy, M.E.P. (登録日: 2014-06-25, 公開日: 2014-10-29, 最終更新日: 2023-12-27)

主引用文献

Kobylarz, M.J.,Grigg, J.C.,Sheldon, J.R.,Heinrichs, D.E.,Murphy, M.E.
SbnG, a Citrate Synthase in Staphylococcus aureus: A NEW FOLD ON AN OLD ENZYME.
J.Biol.Chem., 289:33797-33807, 2014

PubMed Abstract: In response to iron deprivation, Staphylococcus aureus produces staphyloferrin B, a citrate-containing siderophore that delivers iron back to the cell. This bacterium also possesses a second citrate synthase, SbnG, that is necessary for supplying citrate to the staphyloferrin B biosynthetic pathway. We present the structure of SbnG bound to the inhibitor calcium and an active site variant in complex with oxaloacetate. The overall fold of SbnG is structurally distinct from TCA cycle citrate synthases yet similar to metal-dependent class II aldolases. Phylogenetic analyses revealed that SbnG forms a separate clade with homologs from other siderophore biosynthetic gene clusters and is representative of a metal-independent subgroup in the phosphoenolpyruvate/pyruvate domain superfamily. A structural superposition of the SbnG active site to TCA cycle citrate synthases and site-directed mutagenesis suggests a case for convergent evolution toward a conserved catalytic mechanism for citrate production.

PubMed: 25336653
DOI: 10.1074/jbc.M114.603175

実験手法

X-RAY DIFFRACTION (1.85 Å)