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| | <StructureSection load='3k1b' size='340' side='right'caption='[[3k1b]], [[Resolution|resolution]] 4.39Å' scene=''> | | <StructureSection load='3k1b' size='340' side='right'caption='[[3k1b]], [[Resolution|resolution]] 4.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3k1b]] is a 4 chain structure with 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=3K1B OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3K1B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3k1b]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K1B FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k19|3k19]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.39Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3k1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k1b OCA], [http://pdbe.org/3k1b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k1b RCSB], [http://www.ebi.ac.uk/pdbsum/3k1b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k1b ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3k1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k1b OCA], [https://pdbe.org/3k1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k1b RCSB], [https://www.ebi.ac.uk/pdbsum/3k1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k1b ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/OMPF_ECOLI OMPF_ECOLI]] Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.<ref>PMID:19721064</ref> | + | [https://www.uniprot.org/uniprot/OMPF_ECOLI OMPF_ECOLI] Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.<ref>PMID:19721064</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ahn, C]] | + | [[Category: Ahn C]] |
| - | [[Category: CSMP, Center for Structures of Membrane Proteins]]
| + | [[Category: Choe S]] |
| - | [[Category: Choe, S]] | + | [[Category: Kefala G]] |
| - | [[Category: Kefala, G]] | + | [[Category: Krupa M]] |
| - | [[Category: Krupa, M]] | + | [[Category: Kwiatkowski W]] |
| - | [[Category: Kwiatkowski, W]] | + | [[Category: Maslennikov I]] |
| - | [[Category: Maslennikov, I]] | + | |
| - | [[Category: Cell membrane]]
| + | |
| - | [[Category: Cell outer membrane]]
| + | |
| - | [[Category: Center for structures of membrane protein]]
| + | |
| - | [[Category: Csmp]]
| + | |
| - | [[Category: Foscholine-12]]
| + | |
| - | [[Category: Ion transport]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Ompf porin]]
| + | |
| - | [[Category: Phage recognition]]
| + | |
| - | [[Category: Porin]]
| + | |
| - | [[Category: PSI, Protein structure initiative]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Transport]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
OMPF_ECOLI Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The endogenous Escherichia coli porin OmpF was crystallized as an accidental by-product of our efforts to express, purify and crystallize the Escherichia coli integral membrane protein KdpD in the presence of foscholine-12. Foscholine-12 is widely used in membrane protein studies, but no crystal structure of a protein that was both purified and crystallized with this detergent has been reported in PDB. Crystallization screening for KdpD yielded two different crystals of contaminating protein OmpF. Here we report two OmpF structures, the first membrane protein crystal structures for which extraction, purification and crystallization were done exclusively with foscholine-12. The first structure was refined in space group P21 with cell parameters a = 136.7 A, b = 210.5 A, c = 137 A and beta = 100.5 degrees , and the resolution of 3.8 A. The second structure was solved at the resolution of 4.4 A and was refined in the P321 space group, with unit-cell parameters a = 215.5 A, b = 215.5 A, c = 137.5 A and gamma = 120 degrees . Both crystal forms show novel crystal packing, in which the building block is a tetrahedral arrangement of four trimers. Additionally we discuss the use of foscholine-12 for membrane protein crystallization and structure determination, as well as the problem of the OmpF contamination for membrane proteins overexpressed in E. coli.
Structures of the OmpF porin crystallized in the presence of foscholine-12.,Kefala G, Ahn C, Krupa M, Esquivies L, Maslennikov I, Kwiatkowski W, Choe S Protein Sci. 2010 Mar 1. PMID:20196071[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Duval V, Nicoloff H, Levy SB. Combined inactivation of lon and ycgE decreases multidrug susceptibility by reducing the amount of OmpF porin in Escherichia coli. Antimicrob Agents Chemother. 2009 Nov;53(11):4944-8. doi: 10.1128/AAC.00787-09., Epub 2009 Aug 31. PMID:19721064 doi:10.1128/AAC.00787-09
- ↑ Kefala G, Ahn C, Krupa M, Esquivies L, Maslennikov I, Kwiatkowski W, Choe S. Structures of the OmpF porin crystallized in the presence of foscholine-12. Protein Sci. 2010 Mar 1. PMID:20196071 doi:10.1002/pro.369
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