1xck: Difference between revisions

Revision as of 14:24, 28 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:1xck.png

Template:STRUCTURE 1xck

Crystal structure of apo GroELCrystal structure of apo GroEL

Template:ABSTRACT PUBMED 16288915

About this StructureAbout this Structure

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

ReferenceReference

Crystal structure of wild-type chaperonin GroEL., Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H, J Mol Biol. 2005 Dec 9;354(4):940-51. Epub 2005 Oct 21. PMID:16288915

Page seeded by OCA on Mon Jul 28 14:24:05 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1xck.gif|left|200px]]
+{{Seed}}
+[[Image:1xck.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1xck|  PDB=1xck  |  SCENE=  }}
-'''Crystal structure of apo GroEL'''
+===Crystal structure of apo GroEL===
-==Overview==
+<!--
-The 2.9A resolution crystal structure of apo wild-type GroEL was determined for the first time and represents the reference structure, facilitating the study of structural and functional differences observed in GroEL variants. Until now the crystal structure of the mutant Arg13Gly, Ala126Val GroEL was used for this purpose. We show that, due to the mutations as well as to the presence of a crystallographic symmetry, the ring-ring interface was inaccurately described. Analysis of the present structure allowed the definition of structural elements at this interface, essential for understanding the inter-ring allosteric signal transmission. We also show unambiguously that there is no ATP-induced 102 degrees rotation of the apical domain helix I around its helical axis, as previously assumed in the crystal structure of the (GroEL-KMgATP)(14) complex, and analyze the apical domain movements. These results enabled us to compare our structure with other GroEL crystal structures already published, allowing us to suggest a new route through which the allosteric signal for negative cooperativity propagates within the molecule. The proposed mechanism, supported by known mutagenesis data, underlines the importance of the switching of salt bridges.
+The line below this paragraph, {{ABSTRACT_PUBMED_16288915}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16288915 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16288915}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Manakova, E.]]
 [[Category: Chaperonin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:51:25 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:24:05 2008''