2vj4: Difference between revisions

Revision as of 00:44, 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:2vj4.png

Template:STRUCTURE 2vj4

METHYLATED SHIGELLA FLEXNERI MXICMETHYLATED SHIGELLA FLEXNERI MXIC

Template:ABSTRACT PUBMED 18304577

About this StructureAbout this Structure

2VJ4 is a Single protein structure of sequence from Shigella flexneri. Full crystallographic information is available from OCA.

ReferenceReference

Structures of the Shigella flexneri Type 3 Secretion System Protein MxiC Reveal Conformational Variability Amongst Homologues., Deane JE, Roversi P, King C, Johnson S, Lea SM, J Mol Biol. 2008 Feb 4;. PMID:18304577

Page seeded by OCA on Mon Jul 28 00:44:09 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2vj4.jpg|left|200px]]
+{{Seed}}
+[[Image:2vj4.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2vj4|  PDB=2vj4  |  SCENE=  }}
-'''METHYLATED SHIGELLA FLEXNERI MXIC'''
+===METHYLATED SHIGELLA FLEXNERI MXIC===
-==Overview==
+<!--
-Many Gram-negative pathogenic bacteria use a complex macromolecular machine, known as the type 3 secretion system (T3SS), to transfer virulence proteins into host cells. The T3SS is composed of a cytoplasmic bulb, a basal body spanning the inner and outer bacterial membranes, and an extracellular needle. Secretion is regulated by both cytoplasmic and inner membrane proteins that must respond to specific signals in order to ensure that virulence proteins are not secreted before contact with a eukaryotic cell. This negative regulation is mediated, in part, by a family of proteins that are thought to physically block the entrance to the secretion apparatus until an appropriate signal is received following host cell contact. Despite weak sequence homology between proteins of this family, the crystal structures of Shigella flexneri MxiC we present here confirm the conservation of domain topology with the homologue from Yersinia sp. Interestingly, comparison of the Shigella and Yersinia structures reveals a significant structural change that results in substantial domain re-arrangement and opening of one face of the molecule. The conservation of a negatively charged patch on this face suggests it may have a role in binding other components of the T3SS.
+The line below this paragraph, {{ABSTRACT_PUBMED_18304577}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18304577 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18304577}}
 ==About this Structure==
@@ Line 36: / Line 40: @@
 [[Category: Type three secretion system]]
 [[Category: Virulence]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 18:54:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:44:09 2008''