3CKV

Crystal Structure of a Mycobacterial Protein

3CKV の概要

• エントリーDOI: 10.2210/pdb3ckv/pdb
• 関連するPDBエントリー: 3CKJ 3CKN 3KCO 3KCQ
• 分子名称: Putative uncharacterized protein, SULFATE ION, URIDINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: mycobacteria, unknown function
• 由来する生物種: Mycobacterium paratuberculosis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35511.85

構造登録者

Marland, Z.,Rossjohn, J. (登録日: 2008-03-17, 公開日: 2008-07-29, 最終更新日: 2024-02-21)

主引用文献

Fulton, Z.,McAlister, A.,Wilce, M.C.,Brammananth, R.,Zaker-Tabrizi, L.,Perugini, M.A.,Bottomley, S.P.,Coppel, R.L.,Crellin, P.K.,Rossjohn, J.,Beddoe, T.
Crystal structure of a UDP-glucose-specific glycosyltransferase from a Mycobacterium species.
J.Biol.Chem., 283:27881-27890, 2008

PubMed Abstract: Glycosyltransferases (GTs) are a large and ubiquitous family of enzymes that specifically transfer sugar moieties to a range of substrates. Mycobacterium tuberculosis contains a large number of GTs, many of which are implicated in cell wall synthesis, yet the majority of these GTs remain poorly characterized. Here, we report the high resolution crystal structures of an essential GT (MAP2569c) from Mycobacterium avium subsp. paratuberculosis (a close homologue of Rv1208 from M. tuberculosis) in its apo- and ligand-bound forms. The structure adopted the GT-A fold and possessed the characteristic DXD motif that coordinated an Mn(2+) ion. Atypical of most GTs characterized to date, MAP2569c exhibited specificity toward the donor substrate, UDP-glucose. The structure of this ligated complex revealed an induced fit binding mechanism and provided a basis for this unique specificity. Collectively, the structural features suggested that MAP2569c may adopt a "retaining" enzymatic mechanism, which has implications for the classification of other GTs in this large superfamily.

PubMed: 18667419
DOI: 10.1074/jbc.M801853200

実験手法

X-RAY DIFFRACTION (2 Å)