2W04

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

Summary for 2W04

• Entry DOI: 10.2210/pdb2w04/pdb
• Related: 2W02 2W03
• Descriptor: ACSD, CITRATE ANION (3 entities in total)
• Functional Keywords: acsd, pectobacterium chrysanthemi, achromobactin biosynthesis, sspf, metal transport
• Biological source: ERWINIA CHRYSANTHEMI
• Total number of polymer chains: 2
• Total formula weight: 141386.96

Authors

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. (deposition date: 2008-08-08, release date: 2009-01-13, Last modification date: 2024-05-01)

Primary citation

Schmelz, S.,Kadi, N.,Mcmahon, S.A.,Song, L.,Oves-Costales, D.,Oke, M.,Liu, H.,Johnson, K.A.,Carter, L.,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-, 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

Experimental method

X-RAY DIFFRACTION (2.8 Å)