1MDB

CRYSTAL STRUCTURE OF DhbE IN COMPLEX WITH DHB-ADENYLATE

1MDB の概要

• エントリーDOI: 10.2210/pdb1mdb/pdb
• 関連するPDBエントリー: 1AMU 1MD9 1MDF
• 分子名称: 2,3-dihydroxybenzoate-AMP ligase, SULFATE ION, ADENOSINE MONOPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: ligase, adenylation domain, peptide synthetase, antibiotic biosynthesis, siderophore formation
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm : P40871
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60681.60

構造登録者

May, J.J.,Kessler, N.,Marahiel, M.A.,Stubbs, M.T. (登録日: 2002-08-07, 公開日: 2002-09-11, 最終更新日: 2024-02-14)

主引用文献

May, J.J.,Kessler, N.,Marahiel, M.A.,Stubbs, M.T.
Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases.
Proc.Natl.Acad.Sci.USA, 99:12120-12125, 2002

PubMed Abstract: The synthesis of the catecholic siderophore bacillibactin is accomplished by the nonribosomal peptide synthetase (NRPS) encoded by the dhb operon. DhbE is responsible for the initial step in bacillibactin synthesis, the activation of the aryl acid 2,3-dihydroxybenzoate (DHB). The stand-alone adenylation (A) domain DhbE, the structure of which is presented here, exhibits greatest homology to other NRPS A-domains, acyl-CoA ligases and luciferases. It's structure is solved in three different states, without the ligands ATP and DHB (native state), with the product DHB-AMP (adenylate state) and with the hydrolyzed product AMP and DHB (hydrolyzed state). The 59.9-kDa protein folds into two domains, with the active site at the interface between them. In contrast to previous proposals of a major reorientation of the large and small domains on substrate binding, we observe only local structural rearrangements. The structure of the phosphate binding loop could be determined, a motif common to many adenylate-forming enzymes, as well as with bound DHB-adenylate and the hydrolyzed product DHB*AMP. Based on the structure and amino acid sequence alignments, an adapted specificity conferring code for aryl acid activating domains is proposed, allowing assignment of substrate specificity to gene products of previously unknown function.

PubMed: 12221282
DOI: 10.1073/pnas.182156699

実験手法

X-RAY DIFFRACTION (2.15 Å)