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.


1ab6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ab6.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ab6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ab6| PDB=1ab6 | SCENE= }}
{{STRUCTURE_1ab6| PDB=1ab6 | SCENE= }}
-
'''STRUCTURE OF CHEY MUTANT F14N, V86T'''
+
===STRUCTURE OF CHEY MUTANT F14N, V86T===
-
==Overview==
+
<!--
-
The crystal structures of two double mutants (F14N/V21T and F14N/V86T) of the signal transduction protein CheY have been determined to a resolution of 2.4 and 2.2 A, respectively. The structures were solved by molecular replacement and refined to final R values of 18.4 and 19.2%, respectively. Together with urea-denaturation experiments the structures have been used to analyse the effects of mutations where hydrophobic residues are replaced by residues capable of establishing hydrogen bonds. The large increase in stabilization (-12.1 kJ mol-1) of the mutation Phe14Asn arises from two factors: a reverse hydrophobic effect and the formation of a good N-cap at alpha-helix 1. In addition, a forward-backward hydrogen-bonding pattern, resembling an N-capping box and involving Asn14 and Arg18, has been found. The two Val to Thr mutations at the hydrophobic core have different thermodynamic effects: the mutation Val21Thr does not affect the stability of the protein while the mutation Val86Thr causes a small destabilization of 1.7 kJ mol-1. At site 21 a backward side chain-to-backbone hydrogen bond is formed inside alpha-helix 1 with the carbonyl O atom of the i - 4 residue without movement of the mutated side chain. The destabilizing effect of introducing a polar group in the core is efficiently compensated for by the formation of an extra hydrogen bond. At site 86 the new Ogamma atom escapes from the hydrophobic environment by a chi1 rotation into an adjacent hydrophilic cavity to form a new hydrogen bond. In this case the isosteric Val to Thr substitution is disruptive but the loss in stabilization energy is partly compensated by the formation of a hydrogen bond. The two crystal structures described in this work underline the significance of the hydrogen-bond component to protein stability.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9761905}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9761905 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9761905}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
[[Category: Sensory transduction]]
[[Category: Sensory transduction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:04:02 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:31:17 2008''

Revision as of 13:31, 30 June 2008

Image:1ab6.png

Template:STRUCTURE 1ab6

STRUCTURE OF CHEY MUTANT F14N, V86T

Template:ABSTRACT PUBMED 9761905

About this Structure

1AB6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure analysis of two CheY mutants: importance of the hydrogen-bond contribution to protein stability., Wilcock D, Pisabarro MT, Lopez-Hernandez E, Serrano L, Coll M, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):378-85. PMID:9761905

Page seeded by OCA on Mon Jun 30 16:31:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ab6"
Personal tools