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| | <StructureSection load='4d5u' size='340' side='right'caption='[[4d5u]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='4d5u' size='340' side='right'caption='[[4d5u]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4d5u]] is a 6 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=4D5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4D5U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4d5u]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4D5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D5U FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jfb|4jfb]]</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]] 3.5Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4d5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d5u OCA], [http://pdbe.org/4d5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4d5u RCSB], [http://www.ebi.ac.uk/pdbsum/4d5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4d5u 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=4d5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d5u OCA], [https://pdbe.org/4d5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d5u RCSB], [https://www.ebi.ac.uk/pdbsum/4d5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d5u 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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Porin|Porin]] | + | *[[Porin 3D structures|Porin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Escherichia coli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aghajari, N]] | + | [[Category: Aghajari N]] |
| - | [[Category: Chaptal, V]] | + | [[Category: Chaptal V]] |
| - | [[Category: Falson, P]] | + | [[Category: Falson P]] |
| - | [[Category: Flot, D]] | + | [[Category: Flot D]] |
| - | [[Category: Jault, J M]] | + | [[Category: Jault JM]] |
| - | [[Category: Kilburg, A]] | + | [[Category: Kilburg A]] |
| - | [[Category: Wiseman, B]] | + | [[Category: Wiseman B]] |
| - | [[Category: Porin]]
| + | |
| - | [[Category: Structural 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]
Publication Abstract from PubMed
Macromolecule crystal formation can be divided in two major steps: 1. the formation of a nucleus and 2. the growth of this nucleus into a full mature crystal. The latter is well described and understood, while the former remains elusive due to the difficulty to study it and is described by nucleation theories. Here we report the structure of the Escherichiacoli outer membrane porin OmpF in two centered monoclinic space groups. Strikingly, the two crystals originate from the same building block, made of two trimers of OmpF interacting via their rough side. The different crystallization conditions trigger the formation of distinct arrangement of these building blocks, leading to the formation of translational non-crystallographic symmetry (tNCS) in one case, made possible by the loose lateral packing mediated by detergents. In light of nucleation theories, these results allow us to speculate that these two crystals originate from nuclei made of either clusters of building blocks, or already forming columns that later associate laterally using detergents as glue.
Two different centered monoclinic crystals of the E. coli outer-membrane protein OmpF originate from the same building block.,Chaptal V, Kilburg A, Flot D, Wiseman B, Aghajari N, Jault JM, Falson P Biochim Biophys Acta. 2015 Nov 24. pii: S0005-2736(15)00393-4. doi:, 10.1016/j.bbamem.2015.11.021. PMID:26620074[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
- ↑ Chaptal V, Kilburg A, Flot D, Wiseman B, Aghajari N, Jault JM, Falson P. Two different centered monoclinic crystals of the E. coli outer-membrane protein OmpF originate from the same building block. Biochim Biophys Acta. 2015 Nov 24. pii: S0005-2736(15)00393-4. doi:, 10.1016/j.bbamem.2015.11.021. PMID:26620074 doi:http://dx.doi.org/10.1016/j.bbamem.2015.11.021
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