(Q41978309)

English

Identification of the Mg2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY.

scientific article published on April 1999

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scholarly article

1 reference

Europe PubMed Central

14 October 2017

Identification of the Mg2+-binding site in the P-type ATPase and phosphatase members of the HAD (haloacid dehalogenase) superfamily by structural similarity to the response regulator protein CheY. (English)

1 reference

Europe PubMed Central

14 October 2017

author name string

I S Ridder

1

1 reference

Europe PubMed Central

14 October 2017

B W Dijkstra

2

1 reference

Europe PubMed Central

14 October 2017

language of work or name

0 references

publication date

1 April 1999

1 reference

Europe PubMed Central

14 October 2017

Biochemical Journal

1 reference

Europe PubMed Central

14 October 2017

339 ( Pt 2)

1 reference

Europe PubMed Central

14 October 2017

223-226

1 reference

Europe PubMed Central

14 October 2017

The influence of some cations on an adenosine triphosphatase from peripheral nerves

1 reference

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1 reference

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The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold

1 reference

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Three-dimensional map of the plasma membrane H+-ATPase in the open conformation.

1 reference

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Three-dimensional structure of L-2-haloacid dehalogenase from Xanthobacter autotrophicus GJ10 complexed with the substrate-analogue formate

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Bacterial chemotaxis: a field in motion

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Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold

1 reference

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1 reference

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Protein structure comparison by alignment of distance matrices

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Structure of the Mg(2+)-bound form of CheY and mechanism of phosphoryl transfer in bacterial chemotaxis

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Structural conservation in the CheY superfamily

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Magnesium binding to the bacterial chemotaxis protein CheY results in large conformational changes involving its functional surface

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Computer analysis of bacterial haloacid dehalogenases defines a large superfamily of hydrolases with diverse specificity. Application of an iterative approach to database search

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Identifiers

10.1042/0264-6021:3390223

1 reference

Europe PubMed Central

14 October 2017

1 reference

Europe PubMed Central

14 October 2017

1 reference

Europe PubMed Central

14 October 2017

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