4ZVH

Crystal structure of GGDEF domain of the E. coli DosC - form IV

4ZVH の概要

• エントリーDOI: 10.2210/pdb4zvh/pdb
• 分子名称: Diguanylate cyclase DosC, SULFATE ION (2 entities in total)
• 機能のキーワード: oxygen sensing, diguanylate cyclase, cyclic-di-gmp, signaling protein
• 由来する生物種: Escherichia coli K-12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 39993.31

構造登録者

Tarnawski, M.,Barends, T.R.M.,Schlichting, I. (登録日: 2015-05-18, 公開日: 2015-11-11, 最終更新日: 2024-01-10)

主引用文献

Tarnawski, M.,Barends, T.R.,Schlichting, I.
Structural analysis of an oxygen-regulated diguanylate cyclase.
Acta Crystallogr.,Sect.D, 71:2158-2177, 2015

PubMed Abstract: Cyclic di-GMP is a bacterial second messenger that is involved in switching between motile and sessile lifestyles. Given the medical importance of biofilm formation, there has been increasing interest in understanding the synthesis and degradation of cyclic di-GMPs and their regulation in various bacterial pathogens. Environmental cues are detected by sensing domains coupled to GGDEF and EAL or HD-GYP domains that have diguanylate cyclase and phosphodiesterase activities, respectively, producing and degrading cyclic di-GMP. The Escherichia coli protein DosC (also known as YddV) consists of an oxygen-sensing domain belonging to the class of globin sensors that is coupled to a C-terminal GGDEF domain via a previously uncharacterized middle domain. DosC is one of the most strongly expressed GGDEF proteins in E. coli, but to date structural information on this and related proteins is scarce. Here, the high-resolution structural characterization of the oxygen-sensing globin domain, the middle domain and the catalytic GGDEF domain in apo and substrate-bound forms is described. The structural changes between the iron(III) and iron(II) forms of the sensor globin domain suggest a mechanism for oxygen-dependent regulation. The structural information on the individual domains is combined into a model of the dimeric DosC holoprotein. These findings have direct implications for the oxygen-dependent regulation of the activity of the cyclase domain.

PubMed: 26527135
DOI: 10.1107/S139900471501545X

実験手法

X-RAY DIFFRACTION (3.301 Å)