3K9W

Crystal structure of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei with hydrolyzed 3'-dephospho Coenzyme A

3K9W の概要

• エントリーDOI: 10.2210/pdb3k9w/pdb
• 関連するPDBエントリー: 3ikz
• 分子名称: Phosphopantetheine adenylyltransferase, 4'-diphospho pantetheine, ADENINE, ... (7 entities in total)
• 機能のキーワード: niaid, ssgcid, seattle structural genomics center for infectious disease, coenzyme a, coa, biosynthesis, hydrolysis, atp-binding, coenzyme a biosynthesis, nucleotide-binding, nucleotidyltransferase, transferase
• 由来する生物種: Burkholderia pseudomallei
• 細胞内の位置: Cytoplasm : Q3JW91
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21763.67

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2009-10-16, 公開日: 2009-11-03, 最終更新日: 2023-09-06)

主引用文献

Edwards, T.E.,Leibly, D.J.,Bhandari, J.,Statnekov, J.B.,Phan, I.,Dieterich, S.H.,Abendroth, J.,Staker, B.L.,Van Voorhis, W.C.,Myler, P.J.,Stewart, L.J.
Structures of phosphopantetheine adenylyltransferase from Burkholderia pseudomallei.
Acta Crystallogr.,Sect.F, 67:1032-1037, 2011

PubMed Abstract: Phosphopantetheine adenylyltransferase (PPAT) catalyzes the fourth of five steps in the coenzyme A biosynthetic pathway, reversibly transferring an adenylyl group from ATP onto 4'-phosphopantetheine to yield dephospho-coenzyme A and pyrophosphate. Burkholderia pseudomallei is a soil- and water-borne pathogenic bacterium and the etiologic agent of melioidosis, a potentially fatal systemic disease present in southeast Asia. Two crystal structures are presented of the PPAT from B. pseudomallei with the expectation that, because of the importance of the enzyme in coenzyme A biosynthesis, they will aid in the search for defenses against this pathogen. A crystal grown in ammonium sulfate yielded a 2.1 Å resolution structure that contained dephospho-coenzyme A with partial occupancy. The overall structure and ligand-binding interactions are quite similar to other bacterial PPAT crystal structures. A crystal grown at low pH in the presence of coenzyme A yielded a 1.6 Å resolution structure in the same crystal form. However, the experimental electron density was not reflective of fully ordered coenzyme A, but rather was only reflective of an ordered 4'-diphosphopantetheine moiety.

PubMed: 21904046
DOI: 10.1107/S1744309111004349

実験手法

X-RAY DIFFRACTION (1.6 Å)