1P0H

Crystal Structure of Rv0819 from Mycobacterium Tuberculosis MshD-Mycothiol Synthase Coenzyme A Complex

1P0H の概要

• エントリーDOI: 10.2210/pdb1p0h/pdb
• 関連するPDBエントリー: 1OZP
• 分子名称: hypothetical protein Rv0819, COENZYME A, ACETYL COENZYME *A, ... (4 entities in total)
• 機能のキーワード: gnat fold, acetyltransferase, coenzyme a complex, mshd, transferase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35498.43

構造登録者

Vetting, M.W.,Roderick, S.L.,Yu, M.,Blanchard, J.S. (登録日: 2003-04-10, 公開日: 2003-09-09, 最終更新日: 2024-02-14)

主引用文献

Vetting, M.W.,Roderick, S.L.,Yu, M.,Blanchard, J.S.
Crystal structure of mycothiol synthase (Rv0819) from Mycobacterium tuberculosis shows structural homology to the GNAT family of N-acetyltransferases.
Protein Sci., 12:1954-1959, 2003

PubMed Abstract: Mycothiol is the predominant low-molecular weight thiol produced by actinomycetes, including Mycobacterium tuberculosis. The last reaction in the biosynthetic pathway for mycothiol is catalyzed by mycothiol synthase (MshD), which acetylates the cysteinyl amine of cysteine-glucosamine-inositol (Cys-GlcN-Ins). The crystal structure of MshD was determined in the presence of coenzyme A and acetyl-CoA. MshD consists of two tandem-repeated domains, each exhibiting the Gcn5-related N-acetyltransferase (GNAT) fold. These two domains superimpose with a root-mean-square deviation of 1.7 A over 88 residues, and each was found to bind one molecule of coenzyme, although the binding sites are quite different. The C-terminal domain has a similar active site to many GNAT members in which the acetyl group of the coenzyme is presented to an open active site slot. However, acetyl-CoA bound to the N-terminal domain is buried, and is apparently not positioned to promote acetyl transfer. A modeled substrate complex indicates that Cys-GlcN-Ins would only fill a portion of a negatively charged channel located between the two domains. This is the first structure determined for an enzyme involved in the biosynthesis of mycothiol.

PubMed: 12930994
DOI: 10.1110/ps.03153703

実験手法

X-RAY DIFFRACTION (1.6 Å)