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.

1kid

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kid.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kid.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kid| PDB=1kid | SCENE= }}
{{STRUCTURE_1kid| PDB=1kid | SCENE= }}
-
'''GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 191-376, MUTANT WITH ALA 262 REPLACED WITH LEU AND ILE 267 REPLACED WITH MET'''
+
===GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 191-376, MUTANT WITH ALA 262 REPLACED WITH LEU AND ILE 267 REPLACED WITH MET===
-
==Overview==
+
<!--
-
A monomeric peptide fragment of GroEL, consisting of residues 191-376, is a mini-chaperone with a functional chaperoning activity. We have solved the crystal structure at 1.7 A resolution of GroEL(191-376) with a 17-residue N-terminal tag. The N-terminal tag of one molecule binds in the active site of a neighboring molecule in the crystal. This appears to mimic the binding of a peptide substrate molecule. Seven substrate residues are bound in a relatively extended conformation. Interactions between the substrate and the active site are predominantly hydrophobic, but there are also four hydrogen bonds between the main chain of the substrate and side chains of the active site. Although the preferred conformation of a bound substrate is essentially extended, the flexibility of the active site may allow it to accommodate the binding of exposed hydrophobic surfaces in general, such as molten globule-type structures. GroEL can therefore help unfold proteins by binding to a hydrophobic region and exert a binding pressure toward the fully unfolded state, thus acting as an "unfoldase." The structure of the mini-chaperone is very similar to that of residues 191-376 in intact GroEL, so we can build it into GroEL and reconstruct how a peptide can bind to the tetradecamer. A ring of connected binding sites is noted that can explain many aspects of substrate binding and activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9108017}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9108017 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9108017}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Hsp60]]
[[Category: Hsp60]]
[[Category: Phosphorylation]]
[[Category: Phosphorylation]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:47:11 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:23:32 2008''

Revision as of 07:23, 2 July 2008

Image:1kid.png

Template:STRUCTURE 1kid

GROEL (HSP60 CLASS) FRAGMENT (APICAL DOMAIN) COMPRISING RESIDUES 191-376, MUTANT WITH ALA 262 REPLACED WITH LEU AND ILE 267 REPLACED WITH MET

Template:ABSTRACT PUBMED 9108017

About this Structure

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

Reference

A structural model for GroEL-polypeptide recognition., Buckle AM, Zahn R, Fersht AR, Proc Natl Acad Sci U S A. 1997 Apr 15;94(8):3571-5. PMID:9108017

Page seeded by OCA on Wed Jul 2 10:23:32 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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