2FP1

Secreted Chorismate Mutase from Mycobacterium tuberculosis

2FP1 の概要

• エントリーDOI: 10.2210/pdb2fp1/pdb
• 関連するPDBエントリー: 2fp2
• 分子名称: Chorismate mutase, LEAD (II) ION (3 entities in total)
• 機能のキーワード: alpha-helical, isomerase
• 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: 37405.42

構造登録者

Okvist, M.,Dey, R.,Sasso, S.,Grahn, E.,Kast, P.,Krengel, U. (登録日: 2006-01-15, 公開日: 2006-03-28, 最終更新日: 2024-10-30)

主引用文献

Okvist, M.,Dey, R.,Sasso, S.,Grahn, E.,Kast, P.,Krengel, U.
1.6A Crystal Structure of the Secreted Chorismate Mutase from Mycobacterium tuberculosis: Novel Fold Topology Revealed
J.Mol.Biol., 357:1483-1499, 2006

PubMed Abstract: The presence of exported chorismate mutases produced by certain organisms such as Mycobacterium tuberculosis has been shown to correlate with their pathogenicity. As such, these proteins comprise a new group of promising selective drug targets. Here, we report the high-resolution crystal structure of the secreted dimeric chorismate mutase from M. tuberculosis (*MtCM; encoded by Rv1885c), which represents the first 3D-structure of a member of this chorismate mutase family, termed the AroQ(gamma) subclass. Structures are presented both for the unliganded enzyme and for a complex with a transition state analog. The protomer fold resembles the structurally characterized (dimeric) Escherichia coli chorismate mutase domain, but exhibits a new topology, with helix H4 of *MtCM carrying the catalytic site residue missing in the shortened helix H1. Furthermore, the structure of each *MtCM protomer is significantly more compact and only harbors one active site pocket, which is formed entirely by one polypeptide chain. Apart from the structural model, we present evidence as to how the substrate may enter the active site.

PubMed: 16499927
DOI: 10.1016/j.jmb.2006.01.069

実験手法

X-RAY DIFFRACTION (1.55 Å)