2axc

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Crystal structure of ColE7 translocation domain

Structural highlights

2axc is a 1 chain structure with sequence from Escherichia coli str. K-12 substr. W3110. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:GOL, MSE, SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CEA7_ECOLX This plasmid-coded bactericidal protein is an endonuclease active on both single- and double-stranded DNA but with undefined specificity. Colicins are polypeptide toxins produced by and active against E.coli and closely related bacteria.

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

ColE7 is a nuclease-type colicin released from Escherichia coli to kill sensitive bacterial cells by degrading the nucleic acid molecules in their cytoplasm. ColE7 is classified as one of the group A colicins, since the N-terminal translocation domain (T-domain) of the nuclease-type colicins interact with specific membrane-bound or periplasmic Tol proteins during protein import. Here, we show that if the N-terminal tail of ColE7 is deleted, ColE7 (residues 63-576) loses its bactericidal activity against E.coli. Moreover, TolB protein interacts directly with the T-domain of ColE7 (residues 1-316), but not with the N-terminal deleted T-domain (residues 60-316), as detected by co-immunoprecipitation experiments, confirming that the N-terminal tail is required for ColE7 interactions with TolB. The crystal structure of the N-terminal tail deleted ColE7 T-domain was determined by the multi-wavelength anomalous dispersion method at a resolution of 1.7 angstroms. The structure of the ColE7 T-domain superimposes well with the T-domain of ColE3 and TR-domain of ColB, a group A Tol-dependent colicin and a group B TonB-dependent colicin, respectively. The structural resemblance of group A and B colicins implies that the two groups of colicins may share a mechanistic connection during cellular import.

High-resolution crystal structure of a truncated ColE7 translocation domain: implications for colicin transport across membranes.,Cheng YS, Shi Z, Doudeva LG, Yang WZ, Chak KF, Yuan HS J Mol Biol. 2006 Feb 10;356(1):22-31. Epub 2005 Dec 5. PMID:16360169[1]

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

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Citations
1 reviews cite this structure
Cascales et al. (2007)
No citations found

See Also

References

  1. Cheng YS, Shi Z, Doudeva LG, Yang WZ, Chak KF, Yuan HS. High-resolution crystal structure of a truncated ColE7 translocation domain: implications for colicin transport across membranes. J Mol Biol. 2006 Feb 10;356(1):22-31. Epub 2005 Dec 5. PMID:16360169 doi:10.1016/j.jmb.2005.11.056

Contents


PDB ID 2axc

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