3wg5: Difference between revisions
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<StructureSection load='3wg5' size='340' side='right'caption='[[3wg5]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3wg5' size='340' side='right'caption='[[3wg5]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wg5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3wg5]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WG5 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id=' | <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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=3wg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wg5 OCA], [https://pdbe.org/3wg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wg5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wg5 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=3wg5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wg5 OCA], [https://pdbe.org/3wg5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wg5 RCSB], [https://www.ebi.ac.uk/pdbsum/3wg5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wg5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/STOPP_PYRHO STOPP_PYRHO] Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro).<ref>PMID:15611110</ref> <ref>PMID:16574150</ref> <ref>PMID:24121343</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Pyrococcus horikoshii]] | [[Category: Pyrococcus horikoshii OT3]] | ||
[[Category: Fujii | [[Category: Fujii S]] | ||
[[Category: Matsui | [[Category: Matsui I]] | ||
[[Category: Yokoyama | [[Category: Yokoyama H]] | ||
Latest revision as of 16:09, 8 November 2023
1510-N membrane-bound stomatin-specific protease K138A mutant in complex with a substrate peptide under heat treatment1510-N membrane-bound stomatin-specific protease K138A mutant in complex with a substrate peptide under heat treatment
Structural highlights
FunctionSTOPP_PYRHO Protease that cleaves its substrates preferentially near hydrophobic or aromatic amino acid residues. Can degrade casein and the stomatin homolog PH1511 (in vitro).[1] [2] [3] Publication Abstract from PubMedMembrane-bound proteases are involved in various regulatory functions. The N-terminal region of PH1510p (1510-N) from the hyperthermophilic archaeon Pyrococcus horikoshii is a serine protease with a catalytic Ser-Lys dyad (Ser97 and Lys138), and specifically cleaves the C-terminal hydrophobic region of the p-stomatin PH1511p. In a form of human hemolytic anemia known as hereditary stomatocytosis, the stomatin protein is deficient in the erythrocyte membrane due to mis-trafficking. In order to understand the catalytic mechanism of 1510-N in more detail, here the structural and biochemical analysis of 1510-N is reported. Two degraded products were produced via acyl-enzyme intermediates. 1510-N is a thermostable protease, and thus crystallization after heat treatment of the protease-peptide complex was attempted in order to understand the catalytic mechanism of 1510-N. The structure after heat treatment is almost identical to that with no heat treatment. According to the superposition between the structures with heat treatment and with no heat treatment, the N-terminal half of the peptide is superposed well, whereas the C-terminal half of the peptide is slightly deviated. The N-terminal half of the peptide binds to 1510-N more tightly than the C-terminal half of the peptide. The flexible L2 loops of 1510-N cover the peptide, and are involved in the protease activity. Structural and biochemical analysis of a thermostable membrane-bound stomatin-specific protease.,Yokoyama H, Kobayashi D, Takizawa N, Fujii S, Matsui I J Synchrotron Radiat. 2013 Nov;20(Pt 6):933-7. doi: 10.1107/S0909049513021328., Epub 2013 Sep 25. PMID:24121343[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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