2C2A

Structure of the entire cytoplasmic portion of a sensor histidine kinase protein

2C2A の概要

• エントリーDOI: 10.2210/pdb2c2a/pdb
• 分子名称: SENSOR HISTIDINE KINASE, ADENOSINE-5'-DIPHOSPHATE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: histidine kinase, phosphotransfer, phoq, selenomethionyl mad, two-component systems, transferase
• 由来する生物種: THERMOTOGA MARITIMA
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29933.61

構造登録者

Marina, A.,Waldburger, C.D.,Hendrickson, W.A. (登録日: 2005-09-27, 公開日: 2005-11-21, 最終更新日: 2024-10-23)

主引用文献

Marina, A.,Waldburger, C.D.,Hendrickson, W.A.
Structure of the Entire Cytoplasmic Portion of a Sensor Histidine-Kinase Protein.
Embo J., 24:4247-, 2005

PubMed Abstract: The large majority of histidine kinases (HKs) are multifunctional enzymes having autokinase, phosphotransfer and phosphatase activities, and most of these are transmembrane sensor proteins. Sensor HKs possess conserved cytoplasmic phosphorylation and ATP-binding kinase domains. The different enzymatic activities require participation by one or both of these domains, implying the need for different conformational states. The catalytic domains are linked to the membrane through a coiled-coil segment that sometimes includes other domains. We describe here the first crystal structure of the complete cytoplasmic region of a sensor HK, one from the thermophile Thermotoga maritima in complex with ADPbetaN at 1.9 A resolution. The structure reveals previously unidentified functions for several conserved residues and reveals the relative disposition of domains in a state seemingly poised for phosphotransfer. The structure thereby inspires hypotheses for the mechanisms of autophosphorylation, phosphotransfer and response-regulator dephosphorylation, and for signal transduction through the coiled-coil segment. Mutational tests support the functional relevance of interdomain contacts.

PubMed: 16319927
DOI: 10.1038/SJ.EMBOJ.7600886

実験手法

X-RAY DIFFRACTION (1.9 Å)