View source for 3bpp


==1510-N membrane protease K138A mutant specific for a stomatin homolog from Pyrococcus horikoshii==
<StructureSection load='3bpp' size='340' side='right'caption='[[3bpp]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bpp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BPP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=3bpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bpp OCA], [https://pdbe.org/3bpp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bpp RCSB], [https://www.ebi.ac.uk/pdbsum/3bpp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bpp ProSAT]</span></td></tr>
</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> 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bp/3bpp_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bpp ConSurf].
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== Publication Abstract from PubMed ==
Membrane-bound proteases are involved in various regulatory functions. A previous report indicates that the N-terminal region of PH1510 (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 PH1511. According to the crystal structure of the wild-type 1510-N in dimeric form, the active site around Ser97 is in a hydrophobic environment suitable for the hydrophobic substrates. This article reports the crystal structure of the K138A mutant of 1510-N at 2.3 A resolution. The determined structure contains one molecule per asymmetric unit, but 1510-N is active in dimeric form. Two possible sets of dimer were found from the symmetry-related molecules. One dimer is almost the same as the wild-type 1510-N. Another dimer is probably in an inactive form. The L2 loop, which is disordered in the wild-type structure, is significantly kinked at around A-138 in the K138A mutant. Thus Lys138 probably has an important role on the conformation of L2.

Novel dimer structure of a membrane-bound protease with a catalytic Ser-Lys dyad and its linkage to stomatin.,Yokoyama H, Hamamatsu S, Fujii S, Matsui I J Synchrotron Radiat. 2008 May;15(Pt 3):254-7. Epub 2008 Apr 18. PMID:18421152<ref>PMID:18421152</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Pyrococcus horikoshii]]
[[Category: Fujii S]]
[[Category: Hamamatsu S]]
[[Category: Matsui I]]
[[Category: Yokoyama H]]