Colicin E3: Difference between revisions

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==Mechanism of uptake==
==Mechanism of uptake==
{{STRUCTURE_1ujw |  PDB=1ujw  |  SCENE=  }}
ColE3 initially binds to the BtuB vitamin B12 receptor. Formation of this complex leads to the unfolding of the N terminal receptor binding coiled-coil domain of ColE3. <ref> PMID: 17277071 </ref>
ColE3 initially binds to the BtuB vitamin B12 receptor. Formation of this complex leads to the unfolding of the N terminal receptor binding coiled-coil domain of ColE3. <ref> PMID: 17277071 </ref>


The structure shows the complex formed between BtuB and the ColE3 translocation domain <ref> PMID: 14528295 </ref>


==Killing Activities==
==Killing Activities==

Revision as of 19:59, 31 January 2011

Colicin E3 is a type of Colicin, a bacteriocin made by E. Coli which acts against other nearby E. Coli to kill them with its 16s rRNase activity; it digests the 16s ribosomal subunit, ultimately leading to the death of the cell.

Synthesis and releaseSynthesis and release

Mechanism of uptakeMechanism of uptake

PDB ID 1ujw

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1ujw, resolution 2.75Å ()
Ligands: , , , ,
Related: 1nqe, 1jch
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml


ColE3 initially binds to the BtuB vitamin B12 receptor. Formation of this complex leads to the unfolding of the N terminal receptor binding coiled-coil domain of ColE3. [1]

The structure shows the complex formed between BtuB and the ColE3 translocation domain [2]

Killing ActivitiesKilling Activities

ReferencesReferences

  1. Masi M, Vuong P, Humbard M, Malone K, Misra R. Initial steps of colicin E1 import across the outer membrane of Escherichia coli. J Bacteriol. 2007 Apr;189(7):2667-76. Epub 2007 Feb 2. PMID:17277071 doi:10.1128/JB.01448-06
  2. Kurisu G, Zakharov SD, Zhalnina MV, Bano S, Eroukova VY, Rokitskaya TI, Antonenko YN, Wiener MC, Cramer WA. The structure of BtuB with bound colicin E3 R-domain implies a translocon. Nat Struct Biol. 2003 Nov;10(11):948-54. Epub 2003 Oct 5. PMID:14528295 doi:10.1038/nsb997

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