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2AXC

Crystal structure of ColE7 translocation domain

Summary for 2AXC
Entry DOI10.2210/pdb2axc/pdb
Related1M08 7CEI
DescriptorColicin E7, SULFATE ION, GLYCEROL, ... (4 entities in total)
Functional Keywordscolicin, translocation domain, hydrolase
Biological sourceEscherichia coli str. K12 substr.
Total number of polymer chains1
Total formula weight27775.58
Authors
Cheng, Y.S.,Shi, Z.,Doudeva, L.G.,Yang, W.Z.,Chak, K.F.,Yuan, H.S. (deposition date: 2005-09-04, release date: 2006-03-14, Last modification date: 2024-10-23)
Primary citationCheng, Y.S.,Shi, Z.,Doudeva, L.G.,Yang, W.Z.,Chak, K.F.,Yuan, H.S.
High-resolution crystal structure of a truncated ColE7 translocation domain: implications for colicin transport across membranes
J.Mol.Biol., 356:22-31, 2006
Cited by
PubMed Abstract: 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.
PubMed: 16360169
DOI: 10.1016/j.jmb.2005.11.056
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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