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.


1qj8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qj8.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1qj8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qj8| PDB=1qj8 | SCENE= }}
{{STRUCTURE_1qj8| PDB=1qj8 | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE OUTER MEMBRANE PROTEIN OMPX FROM ESCHERICHIA COLI'''
+
===CRYSTAL STRUCTURE OF THE OUTER MEMBRANE PROTEIN OMPX FROM ESCHERICHIA COLI===
-
==Overview==
+
<!--
-
BACKGROUND: The integral outer membrane protein X (OmpX) from Escherichia coli belongs to a family of highly conserved bacterial proteins that promote bacterial adhesion to and entry into mammalian cells. Moreover, these proteins have a role in the resistance against attack by the human complement system. Here we present the first crystal structure of a member of this family. RESULTS: The crystal structure of OmpX from E. coli was determined at 1.9 A resolution using multiple isomorphous replacement. OmpX consists of an eight-stranded antiparallel all-next-neighbor beta barrel. The structure shows two girdles of aromatic amino acid residues and a ribbon of nonpolar residues that attach to the membrane interior. The core of the barrel consists of an extended hydrogen-bonding network of highly conserved residues. OmpX thus resembles an inverse micelle. The structure explains the dramatically improved crystal quality of OmpX containing the mutation His100--&gt;Asn, which made the X-ray analysis possible. The coordination spheres of two bound platinum ions are described. CONCLUSIONS: The OmpX structure shows that within a family of virulence-related membrane proteins, the membrane-spanning part of the protein is much better conserved than the extracellular loops. Moreover, these loops form a protruding beta sheet, the edge of which presumably binds to external proteins. It is suggested that this type of binding promotes cell adhesion and invasion and helps defend against the complement system. Although OmpX has the same beta-sheet topology as the structurally related outer membrane protein A (OmpA), their barrels differ with respect to the shear numbers and internal hydrogen-bonding networks.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10545325}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10545325 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10545325}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Integral membrane protein]]
[[Category: Integral membrane protein]]
[[Category: Platinum complex structure]]
[[Category: Platinum complex structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:20:26 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:12:51 2008''

Revision as of 03:12, 28 July 2008

Image:1qj8.png

Template:STRUCTURE 1qj8

CRYSTAL STRUCTURE OF THE OUTER MEMBRANE PROTEIN OMPX FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 10545325

About this Structure

1QJ8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence., Vogt J, Schulz GE, Structure. 1999 Oct 15;7(10):1301-9. PMID:10545325

Page seeded by OCA on Mon Jul 28 06:12:51 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qj8"
Personal tools