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Structure paper

TitleAtomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase.
Journal, issue, pagesScience, Vol. 352, Issue 6293, Page 1542-1547, Year 2016
Publish dateJun 24, 2016
AuthorsKliment A Verba / Ray Yu-Ruei Wang / Akihiko Arakawa / Yanxin Liu / Mikako Shirouzu / Shigeyuki Yokoyama / David A Agard /
PubMed AbstractThe Hsp90 molecular chaperone and its Cdc37 cochaperone help stabilize and activate more than half of the human kinome. However, both the mechanism by which these chaperones assist their "client" ...The Hsp90 molecular chaperone and its Cdc37 cochaperone help stabilize and activate more than half of the human kinome. However, both the mechanism by which these chaperones assist their "client" kinases and the reason why some kinases are addicted to Hsp90 while closely related family members are independent are unknown. Our structural understanding of these interactions is lacking, as no full-length structures of human Hsp90, Cdc37, or either of these proteins with a kinase have been elucidated. Here we report a 3.9 angstrom cryo-electron microscopy structure of the Hsp90-Cdc37-Cdk4 kinase complex. Surprisingly, the two lobes of Cdk4 are completely separated with the β4-β5 sheet unfolded. Cdc37 mimics part of the kinase N lobe, stabilizing an open kinase conformation by wedging itself between the two lobes. Finally, Hsp90 clamps around the unfolded kinase β5 strand and interacts with exposed N- and C-lobe interfaces, protecting the kinase in a trapped unfolded state. On the basis of this structure and an extensive amount of previously collected data, we propose unifying conceptual and mechanistic models of chaperone-kinase interactions.
External linksScience / PubMed:27339980 / PubMed Central
MethodsEM (single particle)
Resolution3.9 - 10.0 Å
Structure data

3337

5fwk

EMDB-3337: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex
PDB-5fwk: Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex
Method: EM (single particle) / Resolution: 3.9 Å

EMDB-3338:
Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex
Method: EM (single particle) / Resolution: 4.0 Å

EMDB-3339:
Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex
Method: EM (single particle) / Resolution: 5.6 Å

3340

5fwp

EMDB-3340: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex
PDB-5fwp: Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex
Method: EM (single particle) / Resolution: 7.2 Å

3341

5fwl

EMDB-3341: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex
PDB-5fwl: Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex
Method: EM (single particle) / Resolution: 9.0 Å

3342

5fwm

EMDB-3342: Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex
PDB-5fwm: Atomic cryoEM structure of Hsp90-Cdc37-Cdk4 complex
Method: EM (single particle) / Resolution: 8.0 Å

EMDB-3343:
Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex
Method: EM (single particle) / Resolution: 8.0 Å

EMDB-3344:
Atomic cryoEM structure of Hsp90/Cdc37/Cdk4 complex
Method: EM (single particle) / Resolution: 10.0 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / HSP90 / CDC37 / CDK4 / CHAPERONE / KINASE / UNFOLDING

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