5ld9: Difference between revisions
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<StructureSection load='5ld9' size='340' side='right'caption='[[5ld9]], [[Resolution|resolution]] 1.73Å' scene=''> | <StructureSection load='5ld9' size='340' side='right'caption='[[5ld9]], [[Resolution|resolution]] 1.73Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5ld9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[5ld9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_furiosus_DSM_3638 Pyrococcus furiosus DSM 3638]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LD9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LD9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.733Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ld9 OCA], [https://pdbe.org/5ld9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ld9 RCSB], [https://www.ebi.ac.uk/pdbsum/5ld9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ld9 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ld9 OCA], [https://pdbe.org/5ld9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ld9 RCSB], [https://www.ebi.ac.uk/pdbsum/5ld9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ld9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/JAMM1_PYRFU JAMM1_PYRFU] Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. In vitro, is also able to cleave non-physiological ubiquitin (Ub) substrates, such as 'Met1-', 'Lys48-', and 'Lys63'-linked Ub dimers (Ub2), and to remove Ub tags from diverse proteins.<ref>PMID:28479062</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pyrococcus furiosus DSM 3638]] | ||
[[Category: Cao | [[Category: Cao S]] | ||
[[Category: Engilberge | [[Category: Engilberge S]] | ||
[[Category: Franzetti | [[Category: Franzetti B]] | ||
[[Category: Gabel | [[Category: Gabel F]] | ||
[[Category: Girard | [[Category: Girard E]] | ||
[[Category: Maupin-Furlow | [[Category: Maupin-Furlow JA]] | ||
Latest revision as of 14:21, 3 January 2024
Structure of deubiquitinating enzyme homolog, Pyrococcus furiosus JAMM1.Structure of deubiquitinating enzyme homolog, Pyrococcus furiosus JAMM1.
Structural highlights
FunctionJAMM1_PYRFU Metalloprotease that displays desampylase (DSAMP) activity, cleaving ubiquitin-like small archaeal modifier proteins (SAMP1, SAMP2 and SAMP3) from protein conjugates (isopeptide- and linear-linked). Thus, likely regulates sampylation and the pools of 'free' SAMP available for protein modification. In vitro, is also able to cleave non-physiological ubiquitin (Ub) substrates, such as 'Met1-', 'Lys48-', and 'Lys63'-linked Ub dimers (Ub2), and to remove Ub tags from diverse proteins.[1] Publication Abstract from PubMedJAMM/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-A 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 alpha2-helix structural element that is conserved and crucial for binding and removing the Ubl SAMP2 tag. Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPN+ Proteases.,Cao S, Engilberge S, Girard E, Gabel F, Franzetti B, Maupin-Furlow JA Structure. 2017 May 4. pii: S0969-2126(17)30103-X. doi:, 10.1016/j.str.2017.04.002. PMID:28479062[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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