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9ME8

Co-crystal structure of maltose binding protein (MBP)-human SENP3 fusion protein in complex with PELP1 peptide

Summary for 9ME8
Entry DOI10.2210/pdb9me8/pdb
Related PRD IDPRD_900010
DescriptorMaltose/maltodextrin-binding periplasmic protein,Sentrin-specific protease 3, Proline-, glutamic acid- and leucine-rich protein 1, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (5 entities in total)
Functional Keywordscysteine protease, sumo maturation, rixosome, ribosome biogenesis, hydrolase
Biological sourceHomo sapiens (human)
More
Total number of polymer chains2
Total formula weight74511.45
Authors
Kaminski, A.M.,Gordon, J.,Pedersen, L.C.,Stanley, R.E. (deposition date: 2024-12-06, release date: 2025-08-06)
Primary citationGordon, J.,Kaminski, A.M.,Bommu, S.R.,Skrajna, A.,Petrovich, R.M.,Pedersen, L.C.,McGinty, R.K.,Warren, A.J.,Stanley, R.E.
PELP1 coordinates the modular assembly and enzymatic activity of the rixosome complex.
Sci Adv, 11:eadw4603-eadw4603, 2025
Cited by
PubMed Abstract: The rixosome is a large multisubunit complex that initiates RNA decay during critical nuclear transactions including ribosome assembly and heterochromatin maintenance. The overall architecture of the complex remains undefined because several subunits contain intrinsically disordered regions (IDRs). Here, we combined structural and functional approaches to establish PELP1 as the central scaffold of the rixosome upon which the enzymatic subunits modularly assemble. The C-terminal half of PELP1 is composed of a proline-rich IDR that mediates association with the AAA-ATPase MDN1, histones, and the SUMO-specific protease SENP3. The PELP1 IDR contains a glutamic acid-rich region that we establish can chaperone the histone octamer in vitro. Last, the x-ray structure of a small linear motif (SLiM) from the PELP IDR bound to SENP3 reveals how PELP1 allosterically activates SUMO protease activity. This work provides an integrated structural model for understanding the rixosome's dynamic architecture and how it modularly coordinates several cellular functions.
PubMed: 40712028
DOI: 10.1126/sciadv.adw4603
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.93 Å)
Structure validation

243911

건을2025-10-29부터공개중

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