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1cei

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Revision as of 08:40, 24 December 2014

STRUCTURE DETERMINATION OF THE COLICIN E7 IMMUNITY PROTEIN (IMME7) THAT BINDS SPECIFICALLY TO THE DNASE-TYPE COLICIN E7 AND INHIBITS ITS BACTERIOCIDAL ACTIVITY

Structural highlights

1cei is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[IMM7_ECOLX] This protein is able to protect a cell, which harbors the plasmid ColE7 encoding colicin E7, against colicin E7, it binds specifically to the DNase-type colicin and inhibits its bactericidal activity. Dimeric ImmE7 may possess a RNase activity that cleaves its own mRNA at a specific site and thus autoregulates translational expression of the downstream ceiE7 gene as well as degradation of the upstream ceaE7 mRNA.

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 immunity protein of colicin E7 (ImmE7) can bind specifically to the DNase-type colicin E7 and inhibit its bactericidal activity. Here we report the 1.8-angstrom crystal structure of the ImmE7 protein. This is the first x-ray structure determined in the superfamily of colicin immunity proteins. The ImmE7 protein consists of four antiparallel alpha-helices, folded in a topology similar to the architecture of a four-helix bundle structure. A region rich in acidic residues is identified. This negatively charged area has the greatest variability within the family of DNase-type immunity proteins; thus, it seems likely that this area is involved in specific binding to colicin. Based on structural, genetic, and kinetic data, we suggest that all the DNase-type immunity proteins, as well as colicins, share a "homologous-structural framework" and that specific interaction between a colicin and its cognate immunity protein relies upon how well these two proteins' charged residues match on the interaction surface, thus leading to specific immunity of the colicin.

The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface.,Chak KF, Safo MK, Ku WY, Hsieh SY, Yuan HS Proc Natl Acad Sci U S A. 1996 Jun 25;93(13):6437-42. PMID:8692833^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Chak KF, Safo MK, Ku WY, Hsieh SY, Yuan HS. The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface. Proc Natl Acad Sci U S A. 1996 Jun 25;93(13):6437-42. PMID:8692833

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cei"

@@ Line 5: / Line 5: @@
 </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=1cei FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cei OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cei RCSB], [http://www.ebi.ac.uk/pdbsum/1cei PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/IMM7_ECOLX IMM7_ECOLX]] This protein is able to protect a cell, which harbors the plasmid ColE7 encoding colicin E7, against colicin E7, it binds specifically to the DNase-type colicin and inhibits its bactericidal activity. Dimeric ImmE7 may possess a RNase activity that cleaves its own mRNA at a specific site and thus autoregulates translational expression of the downstream ceiE7 gene as well as degradation of the upstream ceaE7 mRNA.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1cei

From Proteopedia

Revision as of 08:40, 24 December 2014

STRUCTURE DETERMINATION OF THE COLICIN E7 IMMUNITY PROTEIN (IMME7) THAT BINDS SPECIFICALLY TO THE DNASE-TYPE COLICIN E7 AND INHIBITS ITS BACTERIOCIDAL ACTIVITY

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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