5lda: Difference between revisions
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==Structure of deubiquitinating enzyme homolog (Pyrococcus furiosus JAMM1) in complex with ubiquitin-like SAMP2.== | |||
<StructureSection load='5lda' size='340' side='right' caption='[[5lda]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5lda]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LDA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LDA FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lda OCA], [http://pdbe.org/5lda PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lda RCSB], [http://www.ebi.ac.uk/pdbsum/5lda PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lda ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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-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<ref>PMID:28479062</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5lda" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cao, S]] | |||
[[Category: Engilberge, S]] | |||
[[Category: Franzetti, B]] | |||
[[Category: Gabel, F]] | |||
[[Category: Girard, E]] | |||
[[Category: Maupin-Furlow, J A]] | |||
[[Category: Cell cycle]] | |||
[[Category: Deubiquitination]] | |||
[[Category: Jamm/mpn+]] | |||
[[Category: Metalloprotease]] | |||
[[Category: Ubiquitin-like protein]] | |||
