The arginine finger of the Bloom syndrome protein: its structural organization and its role in energy coupling. (Q36168680)

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4 January 2020

title

The arginine finger of the Bloom syndrome protein: its structural organization and its role in energy coupling (English)

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4 January 2020

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3

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author name string

Hua Ren

1

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4 January 2020

Shuo-Xing Dou

2

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4 January 2020

Ye Yang

4

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4 January 2020

Peng-Ye Wang

5

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4 January 2020

Mounira Amor-Gueret

6

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4 January 2020

Xu Guang Xi

7

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language of work or name

English

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publication date

30 August 2007

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4 January 2020

published in

Nucleic Acids Research

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volume

35

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4 January 2020

page(s)

6029-6041

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4 January 2020

issue

18

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Structure and mechanism of helicases and nucleic acid translocases

4 January 2020

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Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase

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The enzymatic activities of the Werner syndrome protein are disabled by the amino acid polymorphism R834C.

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Characterization and mutational analysis of the RecQ core of the bloom syndrome protein

1 October 2017

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Vanadate inhibits the ATPase activity and DNA binding capability of bacterial MutS. A structural model for the vanadate-MutS interaction at the Walker A motif

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Site-directed mutagenesis of motif III in PcrA helicase reveals a role in coupling ATP hydrolysis to strand separation.

1 October 2017

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DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase

1 October 2017

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Oligomeric ring structure of the Bloom's syndrome helicase

1 October 2017

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Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism

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12 December 2020

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12 December 2020

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Identifiers

DOI

10.1093/NAR/GKM544

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4 January 2020

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