1q9g

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(New page: 200px<br /><applet load="1q9g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q9g" /> '''NMR STRUCTURE OF THE OUTER MEMBRANE PROTEIN ...)
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'''NMR STRUCTURE OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES'''<br />
'''NMR STRUCTURE OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES'''<br />
==Overview==
==Overview==
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The structure of the integral membrane protein OmpX from Escherichia coli, reconstituted in 60 kDa DHPC micelles (OmpX/DHPC) was calculated from 526, NOE upper limit distance constraints. The structure determination was, based on complete sequence-specific assignments for the amide protons and, the Val, Leu, and Ile(delta1) methyl groups in OmpX, which were, selectively protonated on a perdeuterated background. The solution, structure of OmpX in the DHPC micelles consists of a well-defined, eight-stranded antiparallel beta-barrel, with successive pairs of, beta-strands connected by mobile loops. Several long-range NOEs observed, outside of the transmembrane barrel characterize an extension of a, four-stranded beta-sheet beyond the height of the barrel. This protruding, beta-sheet is believed to be involved in intermolecular interactions, responsible for the biological functions of OmpX. The present approach for, de novo structure determination should be quite widely applicable to, membrane proteins reconstituted in mixed micelles with overall molecular, masses up to about 100 kDa, and may also provide a platform for additional, functional studies.
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The structure of the integral membrane protein OmpX from Escherichia coli reconstituted in 60 kDa DHPC micelles (OmpX/DHPC) was calculated from 526 NOE upper limit distance constraints. The structure determination was based on complete sequence-specific assignments for the amide protons and the Val, Leu, and Ile(delta1) methyl groups in OmpX, which were selectively protonated on a perdeuterated background. The solution structure of OmpX in the DHPC micelles consists of a well-defined, eight-stranded antiparallel beta-barrel, with successive pairs of beta-strands connected by mobile loops. Several long-range NOEs observed outside of the transmembrane barrel characterize an extension of a four-stranded beta-sheet beyond the height of the barrel. This protruding beta-sheet is believed to be involved in intermolecular interactions responsible for the biological functions of OmpX. The present approach for de novo structure determination should be quite widely applicable to membrane proteins reconstituted in mixed micelles with overall molecular masses up to about 100 kDa, and may also provide a platform for additional functional studies.
==About this Structure==
==About this Structure==
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1Q9G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q9G OCA].
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1Q9G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q9G OCA].
==Reference==
==Reference==
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[[Category: trosy]]
[[Category: trosy]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:30:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:24 2008''

Revision as of 12:37, 21 February 2008

Image:1q9g.jpg

1q9g

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NMR STRUCTURE OF THE OUTER MEMBRANE PROTEIN OMPX IN DHPC MICELLES

Overview

The structure of the integral membrane protein OmpX from Escherichia coli reconstituted in 60 kDa DHPC micelles (OmpX/DHPC) was calculated from 526 NOE upper limit distance constraints. The structure determination was based on complete sequence-specific assignments for the amide protons and the Val, Leu, and Ile(delta1) methyl groups in OmpX, which were selectively protonated on a perdeuterated background. The solution structure of OmpX in the DHPC micelles consists of a well-defined, eight-stranded antiparallel beta-barrel, with successive pairs of beta-strands connected by mobile loops. Several long-range NOEs observed outside of the transmembrane barrel characterize an extension of a four-stranded beta-sheet beyond the height of the barrel. This protruding beta-sheet is believed to be involved in intermolecular interactions responsible for the biological functions of OmpX. The present approach for de novo structure determination should be quite widely applicable to membrane proteins reconstituted in mixed micelles with overall molecular masses up to about 100 kDa, and may also provide a platform for additional functional studies.

About this Structure

1Q9G is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

NMR structure of the integral membrane protein OmpX., Fernandez C, Hilty C, Wider G, Guntert P, Wuthrich K, J Mol Biol. 2004 Mar 5;336(5):1211-21. PMID:15037080

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