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| | <StructureSection load='3oqc' size='340' side='right'caption='[[3oqc]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='3oqc' size='340' side='right'caption='[[3oqc]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3oqc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OQC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3oqc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OQC FirstGlance]. <br> |
| - | </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=3oqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oqc OCA], [https://pdbe.org/3oqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oqc RCSB], [https://www.ebi.ac.uk/pdbsum/3oqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oqc ProSAT]</span></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]] 2.6Å</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=3oqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oqc OCA], [https://pdbe.org/3oqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oqc RCSB], [https://www.ebi.ac.uk/pdbsum/3oqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oqc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/UFSP2_MOUSE UFSP2_MOUSE]] Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, an ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins.<ref>PMID:17182609</ref> <ref>PMID:21228277</ref>
| + | [https://www.uniprot.org/uniprot/UFSP2_MOUSE UFSP2_MOUSE] Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, an ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins.<ref>PMID:17182609</ref> <ref>PMID:21228277</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Ubiquitin-fold modifier 1 (Ufm1)-specific protease 2 (UfSP2) is a cysteine protease that is responsible for the release of Ufm1 from Ufm1-conjugated cellular proteins, as well as for the generation of mature Ufm1 from its precursor. The 2.6 A resolution crystal structure of mouse UfSP2 reveals that it is composed of two domains. The C-terminal catalytic domain is similar to UfSP1 with Cys(294), Asp(418), His(420), Tyr(282), and a regulatory loop participating in catalysis. The novel N-terminal domain shows a unique structure and plays a role in the recognition of its cellular substrate C20orf116 and thus in the recruitment of UfSP2 to the endoplasmic reticulum, where C20orf116 predominantly localizes. Mutagenesis studies were carried out to provide the structural basis for understanding the loss of catalytic activity observed in a recently identified UfSP2 mutation that is associated with an autosomal dominant form of hip dysplasia.
| + | |
| - | | + | |
| - | Structure of ubiquitin-fold modifier 1-specific protease UfSP2.,Ha BH, Jeon YJ, Shin SC, Tatsumi K, Komatsu M, Tanaka K, Watson CM, Wallis G, Chung CH, Kim EE J Biol Chem. 2011 Mar 25;286(12):10248-57. Epub 2011 Jan 12. PMID:21228277<ref>PMID:21228277</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 3oqc" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Chung, C H]] | + | [[Category: Chung CH]] |
| - | [[Category: Ha, B H]] | + | [[Category: Ha BH]] |
| - | [[Category: Kim, E E]] | + | [[Category: Kim EE]] |
| - | [[Category: Dph motif cys protease]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
UFSP2_MOUSE Thiol protease which recognizes and hydrolyzes the peptide bond at the C-terminal Gly of UFM1, an ubiquitin-like modifier protein bound to a number of target proteins. Does not hydrolyze SUMO1 or ISG15 ubiquitin-like proteins.[1] [2]
References
- ↑ Kang SH, Kim GR, Seong M, Baek SH, Seol JH, Bang OS, Ovaa H, Tatsumi K, Komatsu M, Tanaka K, Chung CH. Two novel ubiquitin-fold modifier 1 (Ufm1)-specific proteases, UfSP1 and UfSP2. J Biol Chem. 2007 Feb 23;282(8):5256-62. Epub 2006 Dec 20. PMID:17182609 doi:http://dx.doi.org/M610590200
- ↑ Ha BH, Jeon YJ, Shin SC, Tatsumi K, Komatsu M, Tanaka K, Watson CM, Wallis G, Chung CH, Kim EE. Structure of ubiquitin-fold modifier 1-specific protease UfSP2. J Biol Chem. 2011 Mar 25;286(12):10248-57. Epub 2011 Jan 12. PMID:21228277 doi:http://dx.doi.org/10.1074/jbc.M110.172171
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