Structural dynamics of the membrane translocation domain of colicin E9 and its interaction with TolB. (Q54544087)

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9 November 2019

title

Structural dynamics of the membrane translocation domain of colicin E9 and its interaction with TolB (English)

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9 November 2019

1

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9 November 2019

Christopher N Penfold

6

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9 November 2019

Nigel J. Clayden

8

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9 November 2019

Richard James

12

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9 November 2019

Geoffrey Robert Moore

13

object named as

Geoffrey R Moore

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9 November 2019

author name string

Sara B-M Whittaker

2

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9 November 2019

Kaeko Tozawa

3

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9 November 2019

Colin MacDonald

4

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9 November 2019

Ruth Boetzel

5

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9 November 2019

Ann Reilly

7

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9 November 2019

Michael J Osborne

9

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9 November 2019

Andrew M Hemmings

10

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9 November 2019

Colin Kleanthous

11

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9 November 2019

language of work or name

English

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publication date

1 May 2002

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Journal of Molecular Biology

9 November 2019

published in

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9 November 2019

volume

318

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9 November 2019

issue

3

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9 November 2019

page(s)

787-804

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Purification and characterization of monomeric Escherichia coli vitamin B12 receptor with high affinity for colicin E3

9 November 2019

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A 76-residue polypeptide of colicin E9 confers receptor specificity and inhibits the growth of vitamin B12-dependent Escherichia coli 113/3 cells

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Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli

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The structure of TolB, an essential component of the tol-dependent translocation system, and its protein-protein interaction with the translocation domain of colicin E9

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Cleavage of colicin D is necessary for cell killing and requires the inner membrane peptidase LepB.

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Processing of DNase domain during translocation of colicin E7 across the membrane of Escherichia coli

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7 January 2021

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Identifiers

DOI

10.1016/S0022-2836(02)00036-0

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9 November 2019

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