2f1v: Difference between revisions

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[[Image:2f1v.gif|left|200px]]
{{Seed}}
[[Image:2f1v.png|left|200px]]


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{{STRUCTURE_2f1v|  PDB=2f1v  |  SCENE=  }}  
{{STRUCTURE_2f1v|  PDB=2f1v  |  SCENE=  }}  


'''Outer membrane protein OmpW'''
===Outer membrane protein OmpW===




==Overview==
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Escherichia coli OmpW belongs to a family of small outer membrane proteins that are widespread in Gram-negative bacteria. Their functions are unknown, but recent data suggest that they may be involved in the protection of bacteria against various forms of environmental stress. To gain insight into the function of these proteins A we have determined the crystal structure of E. coli OmpW to 2.7-A resolution. The structure shows that OmpW forms an 8-stranded beta-barrel with a long and narrow hydrophobic channel that contains a bound n-dodecyl-N,N-dimethylamine-N-oxide detergent molecule. Single channel conductance experiments show that OmpW functions as an ion channel in planar lipid bilayers. The channel activity can be blocked by the addition of n-dodecyl-N,N-dimethylamine-N-oxide. Taken together, the data suggest that members of the OmpW family could be involved in the transport of small hydrophobic molecules across the bacterial outer membrane.
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(as it appears on PubMed at http://www.pubmed.gov), where 16414958 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16414958}}


==About this Structure==
==About this Structure==
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[[Category: Berg, B van den.]]
[[Category: Berg, B van den.]]
[[Category: Outer membrane protein beta barrel]]
[[Category: Outer membrane protein beta barrel]]
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Revision as of 03:58, 28 July 2008

File:2f1v.png

Template:STRUCTURE 2f1v

Outer membrane protein OmpW

Template:ABSTRACT PUBMED 16414958

About this Structure

2F1V is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel., Hong H, Patel DR, Tamm LK, van den Berg B, J Biol Chem. 2006 Mar 17;281(11):7568-77. Epub 2006 Jan 12. PMID:16414958

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