2f1t

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[[Image:2f1t.gif|left|200px]]
[[Image:2f1t.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2f1t |SIZE=350|CAPTION= <scene name='initialview01'>2f1t</scene>, resolution 3.0&Aring;
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The line below this paragraph, containing "STRUCTURE_2f1t", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= ompW ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_2f1t| PDB=2f1t | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1t OCA], [http://www.ebi.ac.uk/pdbsum/2f1t PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f1t RCSB]</span>
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}}
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'''Outer membrane protein OmpW'''
'''Outer membrane protein OmpW'''
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Berg, B van den.]]
[[Category: Berg, B van den.]]
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[[Category: beta barrel]]
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[[Category: Beta barrel]]
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[[Category: outer membrane protein]]
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[[Category: Outer membrane protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:21:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:56:43 2008''
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Revision as of 00:21, 4 May 2008

Image:2f1t.gif

Template:STRUCTURE 2f1t

Outer membrane protein OmpW


Overview

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.

About this Structure

2F1T 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 Page seeded by OCA on Sun May 4 03:21:50 2008

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