The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase (Q27629965)

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English	The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase	scientific article

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PubMed publication ID

11214325

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title

The bacterial conjugation protein TrwB resembles ring helicases and F1-ATPase (English)

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Europe PubMed Central

PubMed publication ID

11214325

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4 November 2019

author

F. Xavier Gomis-Rüth

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1

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Europe PubMed Central

PubMed publication ID

11214325

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4 November 2019

Gabriel Moncalian

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2

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Europe PubMed Central

PubMed publication ID

11214325

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11214325%20AND%20SRC:MED&resulttype=core&format=json

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4 November 2019

Fernando de la Cruz

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6

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PubMed publication ID

11214325

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4 November 2019

Miquel Coll

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7

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PubMed publication ID

11214325

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author name string

Pérez-Luque R

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3

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Europe PubMed Central

PubMed publication ID

11214325

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4 November 2019

González A

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4

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Europe PubMed Central

PubMed publication ID

11214325

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4 November 2019

Cabezón E

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5

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Europe PubMed Central

PubMed publication ID

11214325

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4 November 2019

language of work or name

English

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publication date

1 February 2001

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PubMed publication ID

11214325

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4 November 2019

published in

Nature

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Europe PubMed Central

PubMed publication ID

11214325

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4 November 2019

volume

409

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Europe PubMed Central

PubMed publication ID

11214325

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11214325%20AND%20SRC:MED&resulttype=core&format=json

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4 November 2019

issue

6820

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PubMed publication ID

11214325

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4 November 2019

page(s)

637-641

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PubMed publication ID

11214325

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cites work

Agrobacterium tumefaciens and the susceptible plant cell: a novel adaptation of extracellular recognition and DNA conjugation

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Bacterial conjugative plasmids mobilize DNA transfer between bacteria and yeast

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A conjugation-like mechanism for prespore chromosome partitioning during sporulation in Bacillus subtilis

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Genetic organization of the conjugal DNA processing region of the IncW plasmid R388.

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Characterization of ATP and DNA Binding Activities of TrwB, the Coupling Protein Essential in Plasmid R388 Conjugation

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Genetic evidence of a coupling role for the TraG protein family in bacterial conjugation

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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides

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7 January 2021

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The structure of the E. coli recA protein monomer and polymer

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7 January 2021

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Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7

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Crystal Structure of the δ′ Subunit of the Clamp-Loader Complex of E. coli DNA Polymerase III

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Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein

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Crystal structure of a DExx box DNA helicase

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Crystal structure of the site-specific recombinase, XerD.

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Bacteriophage T7 helicase/primase proteins form rings around single-stranded DNA that suggest a general structure for hexameric helicases

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A Hexameric Helicase Encircles One DNA Strand and Excludes the Other during DNA Unwinding

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DNA is bound within the central hole to one or two of the six subunits of the T7 DNA helicase

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DNA helicases: 'inching forward'.

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Bacteriophage T4 Dda Helicase Translocates in a Unidirectional Fashion on Single-stranded DNA

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The 3′-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase 1 1Edited by M. Gottesman

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The CCP4 suite: programs for protein crystallography

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[37] Patterson superposition and ab initio phasing

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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AMoRe: an automated package for molecular replacement

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SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

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The carboxyl terminus of protein TraD adds specificity and efficiency to F-plasmid conjugative transfer.

1 reference

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Crossref

reference URL

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7 January 2021

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Identifiers

DOI

10.1038/35054586

2 references

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4418202

stated in

Europe PubMed Central

PubMed publication ID

11214325

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11214325%20AND%20SRC:MED&resulttype=core&format=json

retrieved

4 November 2019

Dimensions Publication ID

1003431376

0 references

OpenCitations bibliographic resource ID

4418202

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4418202

PubMed publication ID

11214325

2 references

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

4418202

stated in

Europe PubMed Central

PubMed publication ID

11214325

reference URL

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11214325%20AND%20SRC:MED&resulttype=core&format=json

retrieved

4 November 2019

 

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