1qqo: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1qqo.gif|left|200px]]
{{Seed}}
[[Image:1qqo.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qqo|  PDB=1qqo  |  SCENE=  }}  
{{STRUCTURE_1qqo|  PDB=1qqo  |  SCENE=  }}  


'''E175S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN'''
===E175S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN===




==Overview==
<!--  
ATP binding induces a conformational change in 70-kDa heat shock proteins (Hsp70s) that facilitates release of bound polypeptides. Using the bovine heat shock cognate protein (Hsc70) as a representative of the Hsp70 family, we have characterized the effect of mutations on the coupling between ATP binding and the nucleotide-induced conformational change. Steady-state solution small-angle X-ray scattering and kinetic fluorescence measurements on a 60-kDa fragment of Hsc70 show that point mutations K71M, E175S, D199S, and D206S in the nucleotide binding cleft impair the ability of ATP to induce a conformational change. A secondary mutation in the peptide binding domain, E543K, "rescues" the ATP-induced transition for three of these mutations (E175S/E543K, D199S/E543K, and D206S/E543K) but not for K71M/E543K. Analysis of kinetics of the ATPase cycle confirm that these effects do not result from unexpectedly rapid ATP hydrolysis or slow ATP binding. Crystallographic structures of E175S, D199S, and D206S mutant ATPase fragment proteins show that the mutations do not perturb the tertiary structure of the protein but do significantly alter the protein-ligand interactions, due in part to an apparent charge compensation effect whereby mutating a (probably) negatively charged carboxyl group to a neutral serine displaces a K+ ion from the nucleotide binding cleft in two out of three cases (E175S and D199S but not D206S).
The line below this paragraph, {{ABSTRACT_PUBMED_10451379}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10451379 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_10451379}}


==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Atpase]]
[[Category: Atpase]]
[[Category: Molecular chaperone]]
[[Category: Molecular chaperone]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:35:40 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:01:11 2008''

Revision as of 08:01, 28 July 2008

File:1qqo.png

Template:STRUCTURE 1qqo

E175S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN

Template:ABSTRACT PUBMED 10451379

About this Structure

1QQO is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

Reference

Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein., Johnson ER, McKay DB, Biochemistry. 1999 Aug 17;38(33):10823-30. PMID:10451379

Page seeded by OCA on Mon Jul 28 11:01:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1qqo&oldid=695391"