3T0Z

Hsp90 N-terminal domain bound to ATP

Summary for 3T0Z

• Entry DOI: 10.2210/pdb3t0z/pdb
• Related: 3T0H 3T10 3T1K
• Descriptor: Heat shock protein HSP 90-alpha, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: chaperone, atpase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P07900
• Total number of polymer chains: 1
• Total formula weight: 26188.25

Authors

Li, J. (deposition date: 2011-07-21, release date: 2012-01-25, Last modification date: 2023-11-01)

Primary citation

Li, J.,Sun, L.,Xu, C.,Yu, F.,Zhou, H.,Zhao, Y.,Zhang, J.,Cai, J.,Mao, C.,Tang, L.,Xu, Y.,He, J.
Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90.
Acta Biochim Biophys Sin (Shanghai), 44:300-306, 2012

PubMed Abstract: The activation of molecular chaperone heat-shock protein 90 (Hsp90) is dependent on ATP binding and hydrolysis, which occurs in the N-terminal domains of protein. Here, we have determined three crystal structures of the N-terminal domain of human Hsp90 in native and in complex with ATP and ATP analog, providing a clear view of the catalytic mechanism of ATP hydrolysis by Hsp90. Additionally, the binding of ATP leads the N-terminal domains to be an intermediate state that could be used to partially explain why the isolated N-terminal domain of Hsp90 has very weak ATP hydrolytic activity.

PubMed: 22318716
DOI: 10.1093/abbs/gms001

Experimental method

X-RAY DIFFRACTION (2.192 Å)