2gr7: Difference between revisions

Revision as of 14:43, 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:2gr7.png

Template:STRUCTURE 2gr7

Hia 992-1098Hia 992-1098

Template:ABSTRACT PUBMED 16688217

About this StructureAbout this Structure

2GR7 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

ReferenceReference

Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter., Meng G, Surana NK, St Geme JW 3rd, Waksman G, EMBO J. 2006 Jun 7;25(11):2297-304. Epub 2006 May 11. PMID:16688217

Page seeded by OCA on Tue Jul 29 14:43:28 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2gr7.gif|left|200px]]
+{{Seed}}
+[[Image:2gr7.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2gr7|  PDB=2gr7  |  SCENE=  }}
-'''Hia 992-1098'''
+===Hia 992-1098===
-==Overview==
+<!--
-Autotransporter proteins are defined by the ability to drive their own secretion across the bacterial outer membrane. The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adhesion to the respiratory epithelium. In this report, we present the crystal structure of the C-terminal end of Hia, corresponding to the entire Hia translocator domain and part of the passenger domain (residues 992-1098). This domain forms a beta-barrel with 12 transmembrane beta-strands, including four strands from each subunit. The beta-barrel has a central channel of 1.8 nm in diameter that is traversed by three N-terminal alpha-helices, one from each subunit. Mutagenesis studies demonstrate that the transmembrane portion of the three alpha-helices and the loop region between the alpha-helices and the neighboring beta-strands are essential for stability of the trimeric structure of the translocator domain, and that trimerization of the translocator domain is a prerequisite for translocator activity. Overall, this study provides important insights into the mechanism of translocation in trimeric autotransporters.
+The line below this paragraph, {{ABSTRACT_PUBMED_16688217}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16688217 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16688217}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Protein secretion]]
 [[Category: Trimeric autotransporter]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 05:25:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 14:43:28 2008''