This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2vgx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2vgx.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2vgx.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2vgx| PDB=2vgx | SCENE= }}
{{STRUCTURE_2vgx| PDB=2vgx | SCENE= }}
-
'''STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION TRANSLOCATOR CHAPERONE SYCD'''
+
===STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION TRANSLOCATOR CHAPERONE SYCD===
-
==Overview==
+
<!--
-
Many Gram-negative bacteria use a type III secretion (T3S) system to directly inject effector molecules into eucaryotic cells in order to establish a symbiotic or pathogenic relationship with their host. The translocation of many T3S proteins requires specialized chaperones from the bacterial cytosol. SycD belongs to a class of T3S chaperones that assists the secretion of pore-forming translocators and, specifically chaperones the translocators YopB and YopD from enteropathogenic Yersinia enterocolitica. In addition, SycD is involved in the regulation of virulence factor biosynthesis and secretion. In this study, we present two crystal structures of Y. enterocolitica SycD at 1.95 and 2.6 A resolution, the first experimental structures of a T3S class II chaperone specific for translocators. The fold of SycD is entirely alpha-helical and reveals three tetratricopeptide repeat-like motifs that had been predicted from amino acid sequence. In both structures, SycD forms dimers utilizing residues from the first tetratricopeptide repeat motif. Using site-directed mutagenesis and size exclusion chromatography, we verified that SycD forms head-to-head homodimers in solution. Although in both structures, dimerization largely depends on the same residues, the two assemblies represent alternative dimers that exhibit different monomer orientations and overall shape. In these two distinct head-to-head dimers, both the concave and the convex surface of each monomer are accessible for interactions with the SycD binding partners YopB and YopD. A SycD variant carrying two point mutations in the dimerization interface is properly folded but defective in dimerization. Expression of this stable SycD monomer in Yersinia does not rescue the phenotype of a sycD null mutant, suggesting a physiological relevance of the dimerization interface.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18054956}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18054956 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18054956}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Tetratricopeptide repeat]]
[[Category: Tetratricopeptide repeat]]
[[Category: Type iii secretion]]
[[Category: Type iii secretion]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 18:47:28 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:08:18 2008''

Revision as of 12:08, 27 July 2008

Image:2vgx.png

Template:STRUCTURE 2vgx

STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION TRANSLOCATOR CHAPERONE SYCD

Template:ABSTRACT PUBMED 18054956

About this Structure

2VGX is a Single protein structure of sequence from Yersinia enterocolitica. Full crystallographic information is available from OCA.

Reference

Structure of the Yersinia enterocolitica type III secretion translocator chaperone SycD., Buttner CR, Sorg I, Cornelis GR, Heinz DW, Niemann HH, J Mol Biol. 2008 Jan 25;375(4):997-1012. Epub 2007 Nov 12. PMID:18054956

Page seeded by OCA on Sun Jul 27 15:08:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vgx"
Personal tools