2c2a
From Proteopedia
| Line 26: | Line 26: | ||
[[Category: two-component systems]] | [[Category: two-component systems]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 10:48:42 2007'' |
Revision as of 08:44, 30 October 2007
|
STRUCTURE OF THE ENTIRE CYTOPLASMIC PORTION OF A SENSOR HISTIDINE KINASE PROTEIN
Overview
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, ... [(full description)]
About this Structure
2C2A is a [Single protein] structure of sequence from [Thermotoga maritima] with SO4 and ADP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure of the entire cytoplasmic portion of a sensor histidine-kinase protein., Marina A, Waldburger CD, Hendrickson WA, EMBO J. 2005 Dec 21;24(24):4247-59. Epub 2005 Dec 1. PMID:16319927
Page seeded by OCA on Tue Oct 30 10:48:42 2007
