5LDA

Structure of deubiquitinating enzyme homolog (Pyrococcus furiosus JAMM1) in complex with ubiquitin-like SAMP2.

Summary for 5LDA

• Entry DOI: 10.2210/pdb5lda/pdb
• Descriptor: JAMM1, SAMP2, ZINC ION, ... (5 entities in total)
• Functional Keywords: jamm/mpn+, metalloprotease, deubiquitination, ubiquitin-like protein, cell cycle
• Biological source: Pyrococcus furiosus; More
• Total number of polymer chains: 2
• Total formula weight: 23151.26

Authors

Cao, S.,Engilberge, S.,Girard, E.,Gabel, F.,Franzetti, B.,Maupin-Furlow, J.A. (deposition date: 2016-06-24, release date: 2017-06-21, Last modification date: 2024-11-13)

Primary citation

Cao, S.,Engilberge, S.,Girard, E.,Gabel, F.,Franzetti, B.,Maupin-Furlow, J.A.
Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPN(+) Proteases.
Structure, 25:823-833.e6, 2017

PubMed Abstract: JAMM/MPN metalloproteases cleave (iso)peptide bonds C-terminal to ubiquitin (Ub) and ubiquitin-like protein (Ubl) domains and typically require association with protein partners for activity, which has limited a molecular understanding of enzyme function. To provide an insight, we solved the X-ray crystal structures of a catalytically active Pyrococcus furiosus JAMM/MPN metalloprotease (PfJAMM1) alone and in complex with a Ubl (PfSAMP2) to 1.7- to 1.9-Å resolution. PfJAMM1 was found to have a redox sensitive dimer interface. In the PfJAMM1-bound state of the SAMP2, a Ubl-to-Ub conformational change was detected. Surprisingly, distant homologs of PfJAMM1 were found to be closely related in 3D structure, including the interface for Ubl/Ub binding. From this work, we infer the molecular basis of how JAMM/MPN proteases recognize and cleave Ubl/Ub tags from diverse proteins and highlight an α2-helix structural element that is conserved and crucial for binding and removing the Ubl SAMP2 tag.

PubMed: 28479062
DOI: 10.1016/j.str.2017.04.002

Experimental method

X-RAY DIFFRACTION (1.9 Å)