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5ld9

From Proteopedia

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Structure of deubiquitinating enzyme homolog, Pyrococcus furiosus JAMM1.

Structural highlights

5ld9 is a 2 chain structure with sequence from Pyrococcus furiosus DSM 3638. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.733Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5ld9"

@@ Line 1: / Line 1: @@
 ==Structure of deubiquitinating enzyme homolog, Pyrococcus furiosus JAMM1.==
-<StructureSection load='5ld9' size='340' side='right' caption='[[5ld9]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
+<StructureSection load='5ld9' size='340' side='right'caption='[[5ld9]], [[Resolution|resolution]] 1.73&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ld9]] is a 2 chain structure. 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]] 1.733&#8491;</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='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>
 </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;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Cao, S]]
+[[Category: Large Structures]]
-[[Category: Engilberge, S]]
+[[Category: Pyrococcus furiosus DSM 3638]]
-[[Category: Franzetti, B]]
+[[Category: Cao S]]
-[[Category: Gabel, F]]
+[[Category: Engilberge S]]
-[[Category: Girard, E]]
+[[Category: Franzetti B]]
-[[Category: Maupin-Furlow, J A]]
+[[Category: Gabel F]]
-[[Category: Deubiquitination]]
+[[Category: Girard E]]
-[[Category: Hydrolase]]
+[[Category: Maupin-Furlow JA]]
-[[Category: Isopeptidase]]
-[[Category: Jamm/mpn+]]
-[[Category: Metalloprotease]]

5ld9

From Proteopedia

Current revision

Structure of deubiquitinating enzyme homolog, Pyrococcus furiosus JAMM1.

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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