2xgl: Difference between revisions
No edit summary |
No edit summary |
||
| (8 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==The X-ray structure of the Escherichia coli colicin M immunity protein demonstrates the presence of a disulphide bridge, which is functionally essential== | |||
<StructureSection load='2xgl' size='340' side='right'caption='[[2xgl]], [[Resolution|resolution]] 2.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xgl]] 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=2XGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XGL 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]] 2.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2xgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xgl OCA], [https://pdbe.org/2xgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xgl RCSB], [https://www.ebi.ac.uk/pdbsum/2xgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xgl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/IMMM_ECOLX IMMM_ECOLX] This protein is able to protect a cell, which harbors the plasmid ColBM-Cl139 encoding colicin M, against colicin M. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Colicin M (ColM), which is produced by some Escherichia coli strains to kill competitor strains from the same or related species, was recently shown to inhibit cell-wall peptidoglycan biosynthesis through enzymatic degradation of its lipid II precursor. ColM-producing strains are protected against the toxin they produce by co-expression of a specific immunity protein, named Cmi, whose mode of action still remains to be identified. We here report the resolution of the crystal structure of Cmi, which is composed of 4 beta-strands and 4 alpha-helices. This rather compact structure revealed a disulfide bond between residues Cys31 and Cys107. Interestingly, these two cysteines and several other residues appeared as conserved in the sequences of several proteins of unknown function, belonging to the YebF family, which exhibit 25-35% overall sequence similarity with Cmi. Site-directed mutagenesis was performed to assess the role of these residues in the ColM immunity-conferring activity of Cmi, which showed that the disulfide bond and residues from the C-terminal extremity of the protein were functionally essential. The involvement of DsbA oxidase in the formation of the Cmi disulfide bond is also demonstrated. | |||
X-ray structure and site-directed mutagenesis analysis of the Escherichia coli colicin M immunity protein.,Gerard F, Brooks MA, Barreteau H, Touze T, Graille M, Bouhss A, Blanot D, van Tilbeurgh H, Mengin-Lecreulx D J Bacteriol. 2010 Oct 29. PMID:21037007<ref>PMID:21037007</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2xgl" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
*[[Colicin | *[[Colicin immunity protein 3D structures|Colicin immunity protein 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Barreteau | [[Category: Large Structures]] | ||
[[Category: Blanot | [[Category: Barreteau H]] | ||
[[Category: Bouhss | [[Category: Blanot D]] | ||
[[Category: Brooks | [[Category: Bouhss A]] | ||
[[Category: Gerard | [[Category: Brooks MA]] | ||
[[Category: Graille | [[Category: Gerard F]] | ||
[[Category: Mengin-Lecreulx | [[Category: Graille M]] | ||
[[Category: Tilbeurgh | [[Category: Mengin-Lecreulx D]] | ||
[[Category: Touze | [[Category: Tilbeurgh Hv]] | ||
[[Category: Touze T]] | |||
Latest revision as of 13:39, 16 August 2023
The X-ray structure of the Escherichia coli colicin M immunity protein demonstrates the presence of a disulphide bridge, which is functionally essentialThe X-ray structure of the Escherichia coli colicin M immunity protein demonstrates the presence of a disulphide bridge, which is functionally essential
Structural highlights
FunctionIMMM_ECOLX This protein is able to protect a cell, which harbors the plasmid ColBM-Cl139 encoding colicin M, against colicin M. Publication Abstract from PubMedColicin M (ColM), which is produced by some Escherichia coli strains to kill competitor strains from the same or related species, was recently shown to inhibit cell-wall peptidoglycan biosynthesis through enzymatic degradation of its lipid II precursor. ColM-producing strains are protected against the toxin they produce by co-expression of a specific immunity protein, named Cmi, whose mode of action still remains to be identified. We here report the resolution of the crystal structure of Cmi, which is composed of 4 beta-strands and 4 alpha-helices. This rather compact structure revealed a disulfide bond between residues Cys31 and Cys107. Interestingly, these two cysteines and several other residues appeared as conserved in the sequences of several proteins of unknown function, belonging to the YebF family, which exhibit 25-35% overall sequence similarity with Cmi. Site-directed mutagenesis was performed to assess the role of these residues in the ColM immunity-conferring activity of Cmi, which showed that the disulfide bond and residues from the C-terminal extremity of the protein were functionally essential. The involvement of DsbA oxidase in the formation of the Cmi disulfide bond is also demonstrated. X-ray structure and site-directed mutagenesis analysis of the Escherichia coli colicin M immunity protein.,Gerard F, Brooks MA, Barreteau H, Touze T, Graille M, Bouhss A, Blanot D, van Tilbeurgh H, Mengin-Lecreulx D J Bacteriol. 2010 Oct 29. PMID:21037007[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||
