|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==Structure of deubiquitinating enzyme homolog, Pyrococcus furiosus JAMM1.== | | ==Structure of deubiquitinating enzyme homolog, Pyrococcus furiosus JAMM1.== |
| - | <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 [http://en.wikipedia.org/wiki/Pyrfu Pyrfu]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LD9 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF1070 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr> | + | <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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ld9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ld9 OCA], [http://pdbe.org/5ld9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ld9 RCSB], [http://www.ebi.ac.uk/pdbsum/5ld9 PDBsum], [http://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 == |
| Line 21: |
Line 23: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pyrfu]] | + | [[Category: Large Structures]] |
| - | [[Category: Cao, S]] | + | [[Category: Pyrococcus furiosus DSM 3638]] |
| - | [[Category: Engilberge, S]] | + | [[Category: Cao S]] |
| - | [[Category: Franzetti, B]] | + | [[Category: Engilberge S]] |
| - | [[Category: Gabel, F]] | + | [[Category: Franzetti B]] |
| - | [[Category: Girard, E]] | + | [[Category: Gabel F]] |
| - | [[Category: Maupin-Furlow, J A]] | + | [[Category: Girard E]] |
| - | [[Category: Deubiquitination]]
| + | [[Category: Maupin-Furlow JA]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Isopeptidase]]
| + | |
| - | [[Category: Jamm/mpn+]]
| + | |
| - | [[Category: Metalloprotease]]
| + | |
| Structural highlights
Function
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.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cao S, Engilberge S, Girard E, Gabel F, Franzetti B, Maupin-Furlow JA. Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPN+ Proteases. Structure. 2017 May 4. pii: S0969-2126(17)30103-X. doi:, 10.1016/j.str.2017.04.002. PMID:28479062 doi:http://dx.doi.org/10.1016/j.str.2017.04.002
- ↑ Cao S, Engilberge S, Girard E, Gabel F, Franzetti B, Maupin-Furlow JA. Structural Insight into Ubiquitin-Like Protein Recognition and Oligomeric States of JAMM/MPN+ Proteases. Structure. 2017 May 4. pii: S0969-2126(17)30103-X. doi:, 10.1016/j.str.2017.04.002. PMID:28479062 doi:http://dx.doi.org/10.1016/j.str.2017.04.002
|
