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< | ==Crystal structure of the Colicin I receptor Cir from E.coli== | ||
<StructureSection load='2hdf' size='340' side='right'caption='[[2hdf]], [[Resolution|resolution]] 2.65Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2hdf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HDF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65Å</td></tr> | |||
-- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=OES:N-OCTYL-2-HYDROXYETHYL+SULFOXIDE'>OES</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></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=2hdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hdf OCA], [https://pdbe.org/2hdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hdf RCSB], [https://www.ebi.ac.uk/pdbsum/2hdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hdf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CIRA_ECOLI CIRA_ECOLI] Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hd/2hdf_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2hdf ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Colicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space, where it inserts into the inner membrane and forms a voltage-dependent ion channel. We determined crystal structures of colicin I receptor alone and in complex with the receptor binding domain of colicin Ia. The receptor undergoes large and unusual conformational changes upon colicin binding, opening at the cell surface and positioning the receptor binding domain of colicin Ia directly above it. We modelled the interaction with full-length colicin Ia to show that the channel forming domain is initially positioned 150 A above the cell surface. Functional data using full-length colicin Ia show that colicin I receptor is necessary for cell surface binding, and suggest that the receptor participates in translocation of colicin Ia across the outer membrane. | |||
Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import.,Buchanan SK, Lukacik P, Grizot S, Ghirlando R, Ali MM, Barnard TJ, Jakes KS, Kienker PK, Esser L EMBO J. 2007 May 16;26(10):2594-604. Epub 2007 Apr 26. PMID:17464289<ref>PMID:17464289</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2hdf" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Colicin I receptor|Colicin I receptor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Buchanan | [[Category: Buchanan SK]] | ||
[[Category: Esser | [[Category: Esser L]] | ||
[[Category: Lukacik | [[Category: Lukacik P]] | ||
Latest revision as of 12:10, 6 November 2024
Crystal structure of the Colicin I receptor Cir from E.coliCrystal structure of the Colicin I receptor Cir from E.coli
Structural highlights
FunctionCIRA_ECOLI Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB. 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 PubMedColicin Ia is a 69 kDa protein that kills susceptible Escherichia coli cells by binding to a specific receptor in the outer membrane, colicin I receptor (70 kDa), and subsequently translocating its channel forming domain across the periplasmic space, where it inserts into the inner membrane and forms a voltage-dependent ion channel. We determined crystal structures of colicin I receptor alone and in complex with the receptor binding domain of colicin Ia. The receptor undergoes large and unusual conformational changes upon colicin binding, opening at the cell surface and positioning the receptor binding domain of colicin Ia directly above it. We modelled the interaction with full-length colicin Ia to show that the channel forming domain is initially positioned 150 A above the cell surface. Functional data using full-length colicin Ia show that colicin I receptor is necessary for cell surface binding, and suggest that the receptor participates in translocation of colicin Ia across the outer membrane. Structure of colicin I receptor bound to the R-domain of colicin Ia: implications for protein import.,Buchanan SK, Lukacik P, Grizot S, Ghirlando R, Ali MM, Barnard TJ, Jakes KS, Kienker PK, Esser L EMBO J. 2007 May 16;26(10):2594-604. Epub 2007 Apr 26. PMID:17464289[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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