Structure of a new crystal form of human Hsp70 ATPase domain

Jerzy Osipiuk; Martin A. Walsh; Brian C. Freeman; Richard I. Morimoto; Andrzej Joachimiak

doi:10.1107/S0907444999002103

Structure of a new crystal form of human Hsp70 ATPase domain

Jerzy Osipiuk, Martin A. Walsh, Brian C. Freeman, Richard I. Morimoto, Andrzej Joachimiak^*

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

Abstract

Hsp70 proteins are highly conserved proteins induced by heat shock and other stress conditions. An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl₂. Both crystal forms belong to the orthorhombic space group P2₁2₁2₁, but show no resemblance in unit-cell parameters. Analysis of the crystal structures for both forms shows a 1-2 Å shift of one of the subdomains of the protein. This conformational change could reflect a 'natural' flexibility of the protein which might be relevant to ATP binding and may facilitate the interaction of other proteins with Hsp70 protein.

Original language	English (US)
Pages (from-to)	1105-1107
Number of pages	3
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	55
Issue number	5
DOIs	https://doi.org/10.1107/S0907444999002103
State	Published - May 1999

ASJC Scopus subject areas

Structural Biology

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10.1107/S0907444999002103

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title = "Structure of a new crystal form of human Hsp70 ATPase domain",

abstract = "Hsp70 proteins are highly conserved proteins induced by heat shock and other stress conditions. An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl2. Both crystal forms belong to the orthorhombic space group P212121, but show no resemblance in unit-cell parameters. Analysis of the crystal structures for both forms shows a 1-2 {\AA} shift of one of the subdomains of the protein. This conformational change could reflect a 'natural' flexibility of the protein which might be relevant to ATP binding and may facilitate the interaction of other proteins with Hsp70 protein.",

author = "Jerzy Osipiuk and Walsh, {Martin A.} and Freeman, {Brian C.} and Morimoto, {Richard I.} and Andrzej Joachimiak",

year = "1999",

month = may,

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language = "English (US)",

volume = "55",

pages = "1105--1107",

journal = "Acta Crystallographica Section D: Biological Crystallography",

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publisher = "International Union of Crystallography",

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T1 - Structure of a new crystal form of human Hsp70 ATPase domain

AU - Osipiuk, Jerzy

AU - Walsh, Martin A.

AU - Freeman, Brian C.

AU - Morimoto, Richard I.

AU - Joachimiak, Andrzej

PY - 1999/5

Y1 - 1999/5

N2 - Hsp70 proteins are highly conserved proteins induced by heat shock and other stress conditions. An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl2. Both crystal forms belong to the orthorhombic space group P212121, but show no resemblance in unit-cell parameters. Analysis of the crystal structures for both forms shows a 1-2 Å shift of one of the subdomains of the protein. This conformational change could reflect a 'natural' flexibility of the protein which might be relevant to ATP binding and may facilitate the interaction of other proteins with Hsp70 protein.

AB - Hsp70 proteins are highly conserved proteins induced by heat shock and other stress conditions. An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl2. Both crystal forms belong to the orthorhombic space group P212121, but show no resemblance in unit-cell parameters. Analysis of the crystal structures for both forms shows a 1-2 Å shift of one of the subdomains of the protein. This conformational change could reflect a 'natural' flexibility of the protein which might be relevant to ATP binding and may facilitate the interaction of other proteins with Hsp70 protein.

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DO - 10.1107/S0907444999002103

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AN - SCOPUS:0033136014

SN - 0907-4449

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JF - Acta Crystallographica Section D: Biological Crystallography

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ER -

Structure of a new crystal form of human Hsp70 ATPase domain

Abstract

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ATPase domain of human heat shock 70kDa protein 1

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Structure of a new crystal form of human Hsp70 ATPase domain

Abstract

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Datasets

ATPase domain of human heat shock 70kDa protein 1

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