1fbq: Difference between revisions

Revision as of 03:00, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fbq.png

Template:STRUCTURE 1fbq

HEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE P237K MUTATIONHEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE P237K MUTATION

Template:ABSTRACT PUBMED 11305238

About this StructureAbout this Structure

1FBQ is a Single protein structure of sequence from Kluyveromyces lactis. Full crystallographic information is available from OCA.

ReferenceReference

Proline in alpha-helical kink is required for folding kinetics but not for kinked structure, function, or stability of heat shock transcription factor., Hardy JA, Nelson HC, Protein Sci. 2000 Nov;9(11):2128-41. PMID:11305238

Page seeded by OCA on Tue Jul 1 03:00:32 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1fbq.jpg|left|200px]]
+{{Seed}}
+[[Image:1fbq.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1fbq|  PDB=1fbq  |  SCENE=  }}
-'''HEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE P237K MUTATION'''
+===HEAT SHOCK TRANSCRIPTION FACTOR DNA BINDING DOMAIN CONTAINING THE P237K MUTATION===
-==Overview==
+<!--
-The DNA-binding domain of the yeast heat shock transcription factor (HSF) contains a strictly conserved proline that is at the center of a kink. To define the role of this conserved proline-centered kink, we replaced the proline with a number of other residues. These substitutions did not diminish the ability of the full-length protein to support growth of yeast or to activate transcription, suggesting that the proline at the center of the kink is not conserved for function. The stability of the isolated mutant DNA-binding domains was unaltered from the wild-type, so the proline is not conserved to maintain the stability of the protein. The crystal structures of two of the mutant DNA-binding domains revealed that the helices in the mutant proteins were still kinked after substitution of the proline, suggesting that the proline does not cause the alpha-helical kink. So why are prolines conserved in this and the majority of other kinked alpha-helices if not for structure, function, or stability? The mutant DNA-binding domains are less soluble than wild-type when overexpressed. In addition, the folding kinetics, as measured by stopped-flow fluorescence, is faster for the mutant proteins. These two results support the premise that the presence of the proline is critical for the folding pathway of HSF's DNA-binding domain. The finding may also be more general and explain why kinked helices maintain their prolines.
+The line below this paragraph, {{ABSTRACT_PUBMED_11305238}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11305238 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11305238}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Helical kink]]
 [[Category: Helix-turn-helix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:08:28 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:00:32 2008''