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-Structure paper
Title | Structure of the anaphase-promoting complex/cyclosome interacting with a mitotic checkpoint complex. |
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Journal, issue, pages | Science, Vol. 323, Issue 5920, Page 1477-1481, Year 2009 |
Publish date | Mar 13, 2009 |
Authors | Franz Herzog / Ivana Primorac / Prakash Dube / Peter Lenart / Björn Sander / Karl Mechtler / Holger Stark / Jan-Michael Peters / |
PubMed Abstract | Once all chromosomes are connected to the mitotic spindle (bioriented), anaphase is initiated by the protein ubiquitylation activity of the anaphase-promoting complex/cyclosome (APC/C) and its ...Once all chromosomes are connected to the mitotic spindle (bioriented), anaphase is initiated by the protein ubiquitylation activity of the anaphase-promoting complex/cyclosome (APC/C) and its coactivator Cdc20 (APC/C(Cdc20)). Before chromosome biorientation, anaphase is delayed by a mitotic checkpoint complex (MCC) that inhibits APC/C(Cdc20). We used single-particle electron microscopy to obtain three-dimensional models of human APC/C in various functional states: bound to MCC, to Cdc20, or to neither (apo-APC/C). These experiments revealed that MCC associates with the Cdc20 binding site on APC/C, locks the otherwise flexible APC/C in a "closed" state, and prevents binding and ubiquitylation of a wide range of different APC/C substrates. These observations clarify the structural basis for the inhibition of APC/C by spindle checkpoint proteins. |
External links | Science / PubMed:19286556 / PubMed Central |
Methods | EM (single particle) |
Resolution | 20.0 Å |
Structure data | EMDB-1591: EMDB-1592: |
Source |
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