4XGU

Structure of C. elegans PCH-2

Summary for 4XGU

• Entry DOI: 10.2210/pdb4xgu/pdb
• Descriptor: Putative pachytene checkpoint protein 2, SULFATE ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: meiotic recombination, aaa+ atpase, protein remodeler, atp-binding protein
• Biological source: Caenorhabditis elegans
• Total number of polymer chains: 6
• Total formula weight: 290018.02

Authors

Ye, Q.,Corbett, K.D. (deposition date: 2015-01-02, release date: 2015-05-06, Last modification date: 2024-02-28)

Primary citation

Ye, Q.,Rosenberg, S.C.,Moeller, A.,Speir, J.A.,Su, T.Y.,Corbett, K.D.
TRIP13 is a protein-remodeling AAA+ ATPase that catalyzes MAD2 conformation switching.
Elife, 4:e07367-, 2015

PubMed Abstract: The AAA+ family ATPase TRIP13 is a key regulator of meiotic recombination and the spindle assembly checkpoint, acting on signaling proteins of the conserved HORMA domain family. Here we present the structure of the Caenorhabditis elegans TRIP13 ortholog PCH-2, revealing a new family of AAA+ ATPase protein remodelers. PCH-2 possesses a substrate-recognition domain related to those of the protein remodelers NSF and p97, while its overall hexameric architecture and likely structural mechanism bear close similarities to the bacterial protein unfoldase ClpX. We find that TRIP13, aided by the adapter protein p31(comet), converts the HORMA-family spindle checkpoint protein MAD2 from a signaling-active 'closed' conformer to an inactive 'open' conformer. We propose that TRIP13 and p31(comet) collaborate to inactivate the spindle assembly checkpoint through MAD2 conformational conversion and disassembly of mitotic checkpoint complexes. A parallel HORMA protein disassembly activity likely underlies TRIP13's critical regulatory functions in meiotic chromosome structure and recombination.

PubMed: 25918846
DOI: 10.7554/eLife.07367

Experimental method

X-RAY DIFFRACTION (2.301 Å)