We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1y50

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1y50.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1y50.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1y50| PDB=1y50 | SCENE= }}
{{STRUCTURE_1y50| PDB=1y50 | SCENE= }}
-
'''X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein (Hpr) F29W mutant domain_swapped dimer'''
+
===X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein (Hpr) F29W mutant domain_swapped dimer===
-
==Overview==
+
<!--
-
The study of proteins from extremophilic organisms continues to generate interest in the field of protein folding because paradigms explaining the enhanced stability of these proteins still elude us and such studies have the potential to further our knowledge of the forces stabilizing proteins. We have undertaken such a study with our model protein HPr from a mesophile, Bacillus subtilis, and a thermophile, Bacillus stearothermophilus. We report here the high-resolution structures of the wild-type HPr protein from the thermophile and a variant, F29W. The variant proved to crystallize in two forms: a monomeric form with a structure very similar to the wild-type protein as well as a domain-swapped dimer. Interestingly, the structure of the domain-swapped dimer for HPr is very different from that observed for a homologous protein, Crh, from B.subtilis. The existence of a domain-swapped dimer has implications for amyloid formation and is consistent with recent results showing that the HPr proteins can form amyloid fibrils. We also characterized the conformational stability of the thermophilic HPr proteins using thermal and solvent denaturation methods and have used the high-resolution structures in an attempt to explain the differences in stability between the different HPr proteins. Finally, we present a detailed analysis of the solution properties of the HPr proteins using a variety of biochemical and biophysical methods.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15713472}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15713472 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15713472}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Sridharan, S.]]
[[Category: Sridharan, S.]]
[[Category: Bacillus stearothermophilus f29w mutant domain-swapped dimer]]
[[Category: Bacillus stearothermophilus f29w mutant domain-swapped dimer]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:53:01 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:02:28 2008''

Revision as of 15:02, 28 July 2008

Image:1y50.png

Template:STRUCTURE 1y50

X-ray crystal structure of Bacillus stearothermophilus Histidine phosphocarrier protein (Hpr) F29W mutant domain_swapped dimer

Template:ABSTRACT PUBMED 15713472

About this Structure

1Y50 is a Single protein structure of sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA.

Reference

The HPr proteins from the thermophile Bacillus stearothermophilus can form domain-swapped dimers., Sridharan S, Razvi A, Scholtz JM, Sacchettini JC, J Mol Biol. 2005 Feb 25;346(3):919-31. Epub 2004 Dec 23. PMID:15713472

Page seeded by OCA on Mon Jul 28 18:02:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y50"
Personal tools