2Y79

STRUCTURE OF THE FIRST GAF DOMAIN E87A MUTANT OF MYCOBACTERIUM TUBERCULOSIS DOSS

2Y79 の概要

• エントリーDOI: 10.2210/pdb2y79/pdb
• 関連するPDBエントリー: 2W3D 2W3E 2W3F 2W3G 2W3H
• 分子名称: REDOX SENSOR HISTIDINE KINASE RESPONSE REGULATOR DEVS, PROTOPORPHYRIN IX CONTAINING FE, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: transferase
• 由来する生物種: MYCOBACTERIUM TUBERCULOSIS
• 細胞内の位置: Cytoplasm (Probable): P95194
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34761.06

構造登録者

Cho, H.Y.,Cho, H.J.,Kang, B.S. (登録日: 2011-01-30, 公開日: 2011-02-16, 最終更新日: 2023-12-20)

主引用文献

Cho, H.Y.,Cho, H.J.,Kim, M.H.,Kang, B.S.
Blockage of the Channel to Heme by the E87 Side Chain in the Gaf Domain of Mycobacterium Tuberculosis Doss Confers the Unique Sensitivity of Doss to Oxygen.
FEBS Lett., 585:1873-, 2011

PubMed Abstract: Two sensor kinases, DosS and DosT, are responsible for recognition of hypoxia in Mycobacterium tuberculosis. Both proteins are structurally similar to each other, but DosS is a redox sensor while DosT binds oxygen. The primary difference between the two proteins is the channel to the heme present in their GAF domains. DosS has a channel that is blocked by E87 while DosT has an open channel. Absorption spectra of DosS mutants with an open channel show that they bind oxygen as DosT does when they are exposed to air, while DosT G85E mutant is oxidized similarly to DosS without formation of an oxy-ferrous form. This suggests that oxygen accessibility to heme is the primary factor governing the oxygen-binding properties of these proteins.

PubMed: 21536032
DOI: 10.1016/J.FEBSLET.2011.04.050

実験手法

X-RAY DIFFRACTION (1.8 Å)