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.


6chy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:6chy.gif|left|200px]]
+
{{Seed}}
 +
[[Image:6chy.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_6chy| PDB=6chy | SCENE= }}
{{STRUCTURE_6chy| PDB=6chy | SCENE= }}
-
'''STRUCTURE OF CHEMOTAXIS PROTEIN CHEY'''
+
===STRUCTURE OF CHEMOTAXIS PROTEIN CHEY===
-
==Overview==
+
<!--
-
Position 106 in CheY is highly conserved as an aromatic residue in the response regulator superfamily. In the structure of the wild-type, apo-CheY, Tyr106 is a rotamer whose electron density is observed in both the inside and the outside positions. In the structure of the T87I mutant of CheY, the threonine to isoleucine change at position 87 causes the side chain of Tyr106 to be exclusively restricted to the outside position. In this report we demonstrate that the T87I mutation causes cells to be smooth swimming and non-chemotactic. We also show that another CheY mutant, Y106W, causes cells to be more tumbly than wild-type CheY, and impairs chemotaxis. In the structure of Y106W, the side chain of Trp106 stays exclusively in the inside position. Furthermore, a T87I/Y106W double mutant, which confers the same phenotype as T87I, restricts the side chain of Trp106 to the outside position. The results from these behavioral and structural studies indicate that the rotameric nature of the Tyr106 residue is involved in activation of the CheY molecule. Specifically, CheY's signaling ability correlates with the conformational heterogeneity of the Tyr106 side chain. Our data also suggest that these mutations affect the signal at an event subsequent to phosphorylation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9030562}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9030562 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9030562}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Signal transduction protein]]
[[Category: Signal transduction protein]]
[[Category: Two-component system]]
[[Category: Two-component system]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:39:35 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:15:58 2008''

Revision as of 11:15, 3 July 2008

Image:6chy.png

Template:STRUCTURE 6chy

STRUCTURE OF CHEMOTAXIS PROTEIN CHEY

Template:ABSTRACT PUBMED 9030562

About this Structure

6CHY is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structures of CheY mutants Y106W and T87I/Y106W. CheY activation correlates with movement of residue 106., Zhu X, Rebello J, Matsumura P, Volz K, J Biol Chem. 1997 Feb 21;272(8):5000-6. PMID:9030562

Page seeded by OCA on Thu Jul 3 14:15:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6chy"
Personal tools