5lda

From Proteopedia

(Difference between revisions)

Current revision

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

Structural highlights

5lda 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 1.9Å
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/5lda"

@@ Line 3: / Line 3: @@
 <StructureSection load='5lda' size='340' side='right'caption='[[5lda]], [[Resolution|resolution]] 1.90&Aring;' 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://proteopedia.org/fgij/fg.htm?mol=5LDA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5lda]] 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=5LDA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LDA FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 1.9&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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://proteopedia.org/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>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5lda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lda OCA], [https://pdbe.org/5lda PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lda RCSB], [https://www.ebi.ac.uk/pdbsum/5lda PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lda 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 22: / Line 24: @@
 </StructureSection>
 [[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: Cell cycle]]
+[[Category: Maupin-Furlow JA]]
-[[Category: Deubiquitination]]
-[[Category: Jamm/mpn+]]
-[[Category: Metalloprotease]]
-[[Category: Ubiquitin-like protein]]

5lda

From Proteopedia

Current revision

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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