3b47

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_3b47", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:3b47.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3b47.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3b47| PDB=3b47 | SCENE= }}
{{STRUCTURE_3b47| PDB=3b47 | SCENE= }}
-
'''Periplasmic sensor domain of chemotaxis protein GSU0582'''
+
===Periplasmic sensor domain of chemotaxis protein GSU0582===
-
==Overview==
+
<!--
-
Periplasmic sensor domains from two methyl-accepting chemotaxis proteins from Geobacter sulfurreducens (encoded by genes GSU0935 and GSU0582) were expressed in Escherichia coli. The sensor domains were isolated, purified, characterized in solution, and their crystal structures were determined. In the crystal, both sensor domains form swapped dimers and show a PAS-type fold. The swapped segment consists of two helices of about 45 residues at the N terminus with the hemes located between the two monomers. In the case of the GSU0582 sensor, the dimer contains a crystallographic 2-fold symmetry and the heme is coordinated by an axial His and a water molecule. In the case of the GSU0935 sensor, the crystals contain a non-crystallographic dimer, and surprisingly, the coordination of the heme in each monomer is different; monomer A heme has His-Met ligation and monomer B heme has His-water ligation as found in the GSU0582 sensor. The structures of these sensor domains are the first structures of PAS domains containing covalently bound heme. Optical absorption, electron paramagnetic resonance and NMR spectroscopy have revealed that the heme groups of both sensor domains are high-spin and low-spin in the oxidized and reduced forms, respectively, and that the spin-state interconversion involves a heme axial ligand replacement. Both sensor domains bind NO in their ferric and ferrous forms but bind CO only in the reduced form. The binding of both NO and CO occurs via an axial ligand exchange process, and is fully reversible. The reduction potentials of the sensor domains differ by 95 mV (-156 mV and -251 mV for sensors GSU0582 and GSU0935, respectively). The swapped dimerization of these sensor domains and redox-linked ligand switch might be related to the mechanism of signal transduction by these chemotaxis proteins.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18329666}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18329666 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18329666}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Signaling protein]]
[[Category: Signaling protein]]
[[Category: Unknown function]]
[[Category: Unknown function]]
 +
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:08:14 2008''

Revision as of 12:08, 29 July 2008

Image:3b47.png

Template:STRUCTURE 3b47

Periplasmic sensor domain of chemotaxis protein GSU0582

Template:ABSTRACT PUBMED 18329666

About this Structure

3B47 is a Single protein structure of sequence from Geobacter sulfurreducens. Full crystallographic information is available from OCA.

Reference

Structures and solution properties of two novel periplasmic sensor domains with c-type heme from chemotaxis proteins of Geobacter sulfurreducens: implications for signal transduction., Pokkuluri PR, Pessanha M, Londer YY, Wood SJ, Duke NE, Wilton R, Catarino T, Salgueiro CA, Schiffer M, J Mol Biol. 2008 Apr 11;377(5):1498-517. Epub 2008 Feb 8. PMID:18329666

Page seeded by OCA on Tue Jul 29 15:08:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3b47"
Personal tools