This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1zh4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zh4.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zh4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zh4| PDB=1zh4 | SCENE= }}
{{STRUCTURE_1zh4| PDB=1zh4 | SCENE= }}
-
'''Crystal Structure Of The Mg+2/BeF3-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE'''
+
===Crystal Structure Of The Mg+2/BeF3-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE===
-
==Overview==
+
<!--
-
Bacterial response regulators are key regulatory proteins that function as the final elements of so-called two-component signaling systems. The activities of response regulators in vivo are modulated by phosphorylation that results from interactions between the response regulator and its cognate histidine protein kinase. The level of response regulator phosphorylation, which is regulated by intra-or extracellular signals sensed by the histidine protein kinase, ultimately determines the output response that is initiated or carried out by the response regulator. We have recently hypothesized that in the OmpR/PhoB subfamily of response regulator transcription factors, this activation involves a common mechanism of dimerization using a set of highly conserved residues in the alpha4-beta5-alpha5 face. Here we report the X-ray crystal structures of the regulatory domains of response regulators TorR (1.8 A), Ca(2+)-bound KdpE (2.0 A), and Mg(2+)/BeF(3)(-)-bound KdpE (2.2 A), both members of the OmpR/ PhoB subfamily from Escherichia coli. Both regulatory domains form symmetric dimers in the asymmetric unit that involve the alpha4-beta5-alpha5 face. As observed previously in other OmpR/PhoB response regulators, the dimer interfaces are mediated by highly conserved residues within this subfamily. These results provide further evidence that most all response regulators of the OmpR/ PhoB subfamily share a common mechanism of activation by dimerization.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16322582}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16322582 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16322582}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Transcription factor]]
[[Category: Transcription factor]]
[[Category: Two-component system]]
[[Category: Two-component system]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:36:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Jul 5 16:22:08 2008''

Revision as of 13:22, 5 July 2008

Image:1zh4.png

Template:STRUCTURE 1zh4

Crystal Structure Of The Mg+2/BeF3-Bound Receiver Domain Of Kdp Potassium Transport System Response Regulator KdpE

Template:ABSTRACT PUBMED 16322582

About this Structure

1ZH4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

A common dimerization interface in bacterial response regulators KdpE and TorR., Toro-Roman A, Wu T, Stock AM, Protein Sci. 2005 Dec;14(12):3077-88. PMID:16322582

Page seeded by OCA on Sat Jul 5 16:22:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1zh4"
Personal tools