2W02

Co-complex Structure of Achromobactin Synthetase Protein D (AcsD) with ATP from Pectobacterium Chrysanthemi

2W02 の概要

• エントリーDOI: 10.2210/pdb2w02/pdb
• 関連するPDBエントリー: 2W03 2W04
• 分子名称: ACSD, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: sspf, acsd, achromobactin biosynthesis, metal transport, pectobacterium chrysanthemi
• 由来する生物種: ERWINIA CHRYSANTHEMI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 142365.92

構造登録者

Schmelz, S.,McMahon, S.A.,Kadi, N.,Song, L.,Oves-Costales, D.,Oke, M.,Liu, H.,Johnson, K.A.,Carter, L.,White, M.F.,Challis, G.L.,Naismith, J.H. (登録日: 2008-08-08, 公開日: 2009-01-13, 最終更新日: 2024-05-01)

主引用文献

Schmelz, S.,Kadi, N.,McMahon, S.A.,Song, L.,Oves-Costales, D.,Oke, M.,Liu, H.,Johnson, K.A.,Carter, L.G.,Botting, C.H.,White, M.F.,Challis, G.L.,Naismith, J.H.
AcsD catalyzes enantioselective citrate desymmetrization in siderophore biosynthesis.
Nat. Chem. Biol., 5:174-182, 2009

PubMed Abstract: Bacterial pathogens need to scavenge iron from their host for growth and proliferation during infection. They have evolved several strategies to do this, one being the biosynthesis and excretion of small, high-affinity iron chelators known as siderophores. The biosynthesis of siderophores is an important area of study, not only for potential therapeutic intervention but also to illuminate new enzyme chemistries. Two general pathways for siderophore biosynthesis exist: the well-characterized nonribosomal peptide synthetase (NRPS)-dependent pathway and the NRPS-independent siderophore (NIS) pathway, which relies on a different family of sparsely investigated synthetases. Here we report structural and biochemical studies of AcsD from Pectobacterium (formerly Erwinia) chrysanthemi, an NIS synthetase involved in achromobactin biosynthesis. The structures of ATP and citrate complexes provide a mechanistic rationale for stereospecific formation of an enzyme-bound (3R)-citryladenylate, which reacts with L-serine to form a likely achromobactin precursor. AcsD is a unique acyladenylate-forming enzyme with a new fold and chemical catalysis strategy.

PubMed: 19182782
DOI: 10.1038/nchembio.145

実験手法

X-RAY DIFFRACTION (2.2 Å)