1Y10

Mycobacterial adenylyl cyclase Rv1264, holoenzyme, inhibited state

1Y10 の概要

• エントリーDOI: 10.2210/pdb1y10/pdb
• 関連するPDBエントリー: 1Y11
• 分子名称: Hypothetical protein Rv1264/MT1302, CALCIUM ION, PENTAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: adenylyl cyclase fold, lyase
• 由来する生物種: Mycobacterium tuberculosis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 175016.43

構造登録者

Tews, I.,Findeisen, F.,Sinning, I.,Schultz, A.,Schultz, J.E.,Linder, J.U. (登録日: 2004-11-16, 公開日: 2005-05-24, 最終更新日: 2024-04-03)

主引用文献

Tews, I.,Findeisen, F.,Sinning, I.,Schultz, A.,Schultz, J.E.,Linder, J.U.
The structure of a pH-sensing mycobacterial adenylyl cyclase holoenzyme
Science, 308:1020-1023, 2005

PubMed Abstract: Class III adenylyl cyclases contain catalytic and regulatory domains, yet structural insight into their interactions is missing. We show that the mycobacterial adenylyl cyclase Rv1264 is rendered a pH sensor by its N-terminal domain. In the structure of the inhibited state, catalytic and regulatory domains share a large interface involving catalytic residues. In the structure of the active state, the two catalytic domains rotate by 55 degrees to form two catalytic sites at their interface. Two alpha helices serve as molecular switches. Mutagenesis is consistent with a regulatory role of the structural transition, and we suggest that the transition is regulated by pH.

PubMed: 15890882
DOI: 10.1126/science.1107642

実験手法

X-RAY DIFFRACTION (2.3 Å)