2oj6: Difference between revisions

Revision as of 08:44, 29 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:2oj6.png

Template:STRUCTURE 2oj6

Crystal Structure of Reovirus T3D Attachment Protein Sigma1 head domain D345N mutantCrystal Structure of Reovirus T3D Attachment Protein Sigma1 head domain D345N mutant

Template:ABSTRACT PUBMED 17303562

About this StructureAbout this Structure

2OJ6 is a Single protein structure of sequence from Reovirus sp.. Full crystallographic information is available from OCA.

ReferenceReference

The reovirus sigma1 aspartic acid sandwich: a trimerization motif poised for conformational change., Schelling P, Guglielmi KM, Kirchner E, Paetzold B, Dermody TS, Stehle T, J Biol Chem. 2007 Apr 13;282(15):11582-9. Epub 2007 Feb 15. PMID:17303562

Page seeded by OCA on Tue Jul 29 08:44:03 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2oj6.gif|left|200px]]
+{{Seed}}
+[[Image:2oj6.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2oj6|  PDB=2oj6  |  SCENE=  }}
-'''Crystal Structure of Reovirus T3D Attachment Protein Sigma1 head domain D345N mutant'''
+===Crystal Structure of Reovirus T3D Attachment Protein Sigma1 head domain D345N mutant===
-==Overview==
+<!--
-Reovirus attachment protein sigma1 mediates engagement of receptors on the surface of target cells and undergoes dramatic conformational rearrangements during viral disassembly in the endocytic pathway. The sigma1 protein is a filamentous, trimeric molecule with a globular beta-barrel head domain. An unusual cluster of aspartic acid residues sandwiched between hydrophobic tyrosines is located at the sigma1 subunit interface. A 1.75-A structure of the sigma1 head domain now reveals two water molecules at the subunit interface that are held strictly in position and interact with neighboring residues. Structural and biochemical analyses of mutants affecting the aspartic acid sandwich indicate that these residues and the corresponding chelated water molecules act as a plug to block the free flow of solvent and stabilize the trimer. This arrangement of residues at the sigma1 head trimer interface illustrates a new protein design motif that may confer conformational mobility during cell entry.
+The line below this paragraph, {{ABSTRACT_PUBMED_17303562}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17303562 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17303562}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Greek key motif]]
 [[Category: Trimer]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:01:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:44:03 2008''