We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2avk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2avk.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2avk.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2avk| PDB=2avk | SCENE= }}
{{STRUCTURE_2avk| PDB=2avk | SCENE= }}
-
'''met-azido-DcrH-Hr'''
+
===met-azido-DcrH-Hr===
-
==Overview==
+
<!--
-
The methyl-accepting chemotaxis protein, DcrH, from the anaerobic sulfate-reducing bacterium, Desulfovibrio vulgaris (Hildenborough), has a hemerythrin-like domain, DcrH-Hr, at its C terminus. DcrH-Hr was previously shown to contain a diiron site that binds O2, suggesting an O2-sensing function. X-ray crystal structures of diferric (met-), azido-diferric (azidomet-), and diferrous (deoxy-) DcrH-Hr reveal a "substrate tunnel" distinct from that in invertebrate hemerythrins. This tunnel is proposed to facilitate the rapid autoxidation of oxy-DcrH-Hr and suggests that sensing is triggered by O2 binding and subsequent oxidation of the diferrous active site. The N-terminal loop of DcrH-Hr is highly ordered in both met- and azidomet-DcrH-Hr but is disordered in deoxy-DcrH-Hr. These redox-dependent conformational differences presumably transduce the sensory signal of DcrH-Hr to the neighboring methylation domain in the full-length receptor. Given the putative cytoplasmic localization of its Hr-like O2-sensing domain, DcrH is proposed to serve a role in negative aerotaxis (anaerotaxis).
+
The line below this paragraph, {{ABSTRACT_PUBMED_16866347}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16866347 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16866347}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Silaghi-Dumitrescu, R.]]
[[Category: Silaghi-Dumitrescu, R.]]
[[Category: Hemerythrin-like oxygen sensor]]
[[Category: Hemerythrin-like oxygen sensor]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:31:31 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:28:07 2008''

Revision as of 21:28, 27 July 2008

Image:2avk.png

Template:STRUCTURE 2avk

met-azido-DcrH-Hr

Template:ABSTRACT PUBMED 16866347

About this Structure

2AVK is a Single protein structure of sequence from Desulfovibrio vulgaris. Full crystallographic information is available from OCA.

Reference

Structural basis for O2 sensing by the hemerythrin-like domain of a bacterial chemotaxis protein: substrate tunnel and fluxional N terminus., Isaza CE, Silaghi-Dumitrescu R, Iyer RB, Kurtz DM Jr, Chan MK, Biochemistry. 2006 Aug 1;45(30):9023-31. PMID:16866347

Page seeded by OCA on Mon Jul 28 00:28:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2avk"
Personal tools