Structure of a new crystal form of human Hsp70 ATPase domain.
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 A 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.
Osipiuk
J
J
Argonne National Laboratory, Center for Mechanistic Biology and Biotechnology, 9700 S. Cass Avenue, Argonne, IL 60439, USA.
Walsh
M A
MA
Freeman
B C
BC
Morimoto
R I
RI
Joachimiak
A
A
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry*; D006801:Humans; D008958:Models, Molecular; D010446:Peptide Fragments / Q000737:chemistry*; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
D018840:HSP70 Heat-Shock Proteins; D010446:Peptide Fragments; D000251:Adenosine Triphosphatases