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-Structure paper
タイトル | Structure of the anaphase-promoting complex/cyclosome interacting with a mitotic checkpoint complex. |
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ジャーナル・号・ページ | Science, Vol. 323, Issue 5920, Page 1477-1481, Year 2009 |
掲載日 | 2009年3月13日 |
著者 | Franz Herzog / Ivana Primorac / Prakash Dube / Peter Lenart / Björn Sander / Karl Mechtler / Holger Stark / Jan-Michael Peters / |
PubMed 要旨 | 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. |
リンク | Science / PubMed:19286556 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 20.0 Å |
構造データ | EMDB-1591: EMDB-1592: |
由来 |
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