1col: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1col.gif|left|200px]]


{{Structure
==REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION==
|PDB= 1col |SIZE=350|CAPTION= <scene name='initialview01'>1col</scene>, resolution 2.4&Aring;
<StructureSection load='1col' size='340' side='right'caption='[[1col]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1col]] is a 2 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=1COL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1COL FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1col FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1col OCA], [https://pdbe.org/1col PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1col RCSB], [https://www.ebi.ac.uk/pdbsum/1col PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1col ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/CEA_ECOLX CEA_ECOLX] This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.<ref>PMID:2434951</ref>  Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.<ref>PMID:2434951</ref>
== 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/co/1col_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1col ConSurf].
<div style="clear:both"></div>


'''REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION'''
==See Also==
 
*[[Colicin 3D structures|Colicin 3D structures]]
 
== References ==
==Overview==
<references/>
The E1 subgroup (E1, A, B, IA, IB, K and N) of anti-bacterial toxins called colicins is known to form voltage-dependent channels in lipid bilayers. The crystal structure of the pore-forming domain of colicin A from Escherichia coli has been refined to the diffraction limit of the crystals at 2.4 A resolution by means of molecular dynamics and restrained least-squares methods to a conventional R-factor of 0.18 for all data between 6.0 and 2.4 A resolution. The polypeptide chain of 204 amino acid residues consists of ten alpha-helices organized in a three-layer structure. The helices range in length from 9 to 23 residues with an average length of 125 residues. The packing arrangement of the helices has been analysed; the packing is different from that observed in four-helix bundle proteins. The sites of 83 water molecules have been located and refined. Analysis of the structure provides insights into the mechanism of formation of a voltage-gated channel by the protein. Although it is proposed that substantial tertiary structural changes occur during membrane insertion, the secondary structural elements remain conserved. This idea has been proposed recently for a number of other protein-membrane events and thus may have more general applicability.
__TOC__
 
</StructureSection>
==About this Structure==
1COL is a [[Single protein]] structure of 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=1COL OCA].
 
==Reference==
Refined structure of the pore-forming domain of colicin A at 2.4 A resolution., Parker MW, Postma JP, Pattus F, Tucker AD, Tsernoglou D, J Mol Biol. 1992 Apr 5;224(3):639-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1373773 1373773]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Parker, M W.]]
[[Category: Parker MW]]
[[Category: Pattus, F.]]
[[Category: Pattus F]]
[[Category: Postma, J P.M.]]
[[Category: Postma JPM]]
[[Category: Tsernoglou, D.]]
[[Category: Tsernoglou D]]
[[Category: Tucker, A D.]]
[[Category: Tucker AD]]
[[Category: antibacterial protein]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:26:58 2008''

Latest revision as of 09:44, 7 February 2024

REFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTIONREFINED STRUCTURE OF THE PORE-FORMING DOMAIN OF COLICIN A AT 2.4 ANGSTROMS RESOLUTION

Structural highlights

1col is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CEA_ECOLX This colicin is a channel-forming colicin. This class of transmembrane toxins depolarize the cytoplasmic membrane, leading to dissipation of cellular energy.[1] Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Baty D, Knibiehler M, Verheij H, Pattus F, Shire D, Bernadac A, Lazdunski C. Site-directed mutagenesis of the COOH-terminal region of colicin A: effect on secretion and voltage-dependent channel activity. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1152-6. PMID:2434951
  2. ↑ Baty D, Knibiehler M, Verheij H, Pattus F, Shire D, Bernadac A, Lazdunski C. Site-directed mutagenesis of the COOH-terminal region of colicin A: effect on secretion and voltage-dependent channel activity. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1152-6. PMID:2434951

1col, resolution 2.40Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1col&oldid=4041223"