We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1bxw

From Proteopedia

Revision as of 09:05, 2 May 2008 by OCA (Talk | contribs)
Jump to: navigation, search
Image:1bxw.gif

Template:STRUCTURE 1bxw

OUTER MEMBRANE PROTEIN A (OMPA) TRANSMEMBRANE DOMAIN


Overview

The outer membrane protein A of Escherichia coli (OmpA) is an intensely studied example in the field of membrane protein folding. We have determined the structure of the OmpA transmembrane domain consisting of residues 1-171, by X-ray diffraction analysis, to a resolution of 2.5 A. It consists of a regular, extended eight-stranded beta-barrel and appears to be constructed like an inverse micelle with large water-filled cavities, but does not form a pore. Surprisingly, the cavities seem to be highly conserved during evolution. The structure corroborates the concept that all outer membrane proteins consist of beta-barrels. The structure constitutes a beta-barrel membrane anchor that appears to be the outer membrane equivalent of the single-chain alpha-helix anchor of the inner membrane.

About this Structure

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

Reference

Structure of the outer membrane protein A transmembrane domain., Pautsch A, Schulz GE, Nat Struct Biol. 1998 Nov;5(11):1013-7. PMID:9808047 Page seeded by OCA on Fri May 2 12:05:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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