1Q9J

Structure of polyketide synthase associated protein 5 from Mycobacterium tuberculosis

1Q9J の概要

• エントリーDOI: 10.2210/pdb1q9j/pdb
• 分子名称: Polyketide synthase associated protein 5 (2 entities in total)
• 機能のキーワード: polyketide synthase associated protein; conjugating enzyme papa5; mycobacterium tuberculosis, structural genomics, psi, protein structure initiative, new york sgx research center for structural genomics, nysgxrc, ligase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90931.06

構造登録者

Buglino, J.,Onwueme, K.C.,Quadri, L.E.,Lima, C.D.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2003-08-25, 公開日: 2004-05-25, 最終更新日: 2024-02-14)

主引用文献

Buglino, J.,Onwueme, K.C.,Ferreras, J.A.,Quadri, L.E.,Lima, C.D.
Crystal Structure of PapA5, a Phthiocerol Dimycocerosyl Transferase from Mycobacterium tuberculosis
J.Biol.Chem., 279:30634-30642, 2004

PubMed Abstract: Polyketide-associated protein A5 (PapA5) is an acyltransferase that is involved in production of phthiocerol and phthiodiolone dimycocerosate esters, a class of virulence-enhancing lipids produced by Mycobacterium tuberculosis. Structural analysis of PapA5 at 2.75-A resolution reveals a two-domain structure that shares unexpected similarity to structures of chloramphenicol acetyltransferase, dihydrolipoyl transacetylase, carnitine acetyltransferase, and VibH, a non-ribosomal peptide synthesis condensation enzyme. The PapA5 active site includes conserved histidine and aspartic acid residues that are critical to PapA5 acyltransferase activity. PapA5 catalyzes acyl transfer reactions on model substrates that contain long aliphatic carbon chains, and two hydrophobic channels were observed linking the PapA5 surface to the active site with properties consistent with these biochemical activities and substrate preferences. An additional alpha helix not observed in other acyltransferase structures blocks the putative entrance into the PapA5 active site, indicating that conformational changes may be associated with PapA5 activity. PapA5 represents the first structure solved for a protein involved in polyketide synthesis in Mycobacteria.

PubMed: 15123643
DOI: 10.1074/jbc.M404011200

実験手法

X-RAY DIFFRACTION (2.75 Å)