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New page: left|200px<br /> <applet load="1gt9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gt9, resolution 1.38Å" /> '''HIGH RESOLUTION CRY...
 
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[[Image:1gt9.gif|left|200px]]<br />
<applet load="1gt9" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gt9, resolution 1.38&Aring;" />
'''HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE'''<br />


==Overview==
==High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp)==
Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the, newly identified family of serine-carboxyl proteinases, which also, includes CLN2, a human lysosomal homolog recently implicated in a fatal, neurodegenerative disease. Kumamolysin and its complexes with two aldehyde, inhibitors were crystallized, and their three-dimensional structures were, solved and refined with X-ray data to 1.4 A resolution. As its Pseudomonas, homolog, kumamolysin exhibits a Ser/Glu/Asp catalytic triad with, particularly short interconnecting hydrogen bonds and an oxyanion hole, enabling the reactive serine to attack substrate peptide bonds at quite, acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?12057200 (full description)]]
<StructureSection load='1gt9' size='340' side='right'caption='[[1gt9]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gt9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GT9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GT9 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]] 1.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1gt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gt9 OCA], [https://pdbe.org/1gt9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gt9 RCSB], [https://www.ebi.ac.uk/pdbsum/1gt9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gt9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8RR56_9BACI Q8RR56_9BACI]
== 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/gt/1gt9_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=1gt9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the newly identified family of serine-carboxyl proteinases, which also includes CLN2, a human lysosomal homolog recently implicated in a fatal neurodegenerative disease. Kumamolysin and its complexes with two aldehyde inhibitors were crystallized, and their three-dimensional structures were solved and refined with X-ray data to 1.4 A resolution. As its Pseudomonas homolog, kumamolysin exhibits a Ser/Glu/Asp catalytic triad with particularly short interconnecting hydrogen bonds and an oxyanion hole enabling the reactive serine to attack substrate peptide bonds at quite acidic pH. An additional Glu/Trp pair, unique to kumamolysin, might further facilitate proton delocalization during nucleophilic attack, in particular at high temperature.


==About this Structure==
The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase.,Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W Structure. 2002 Jun;10(6):865-76. PMID:12057200<ref>PMID:12057200</ref>
1GT9 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_sp._mn-32 Bacillus sp. mn-32]] with CA and SO4 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GT9 OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The 1.4 a crystal structure of kumamolysin: a thermostable serine-carboxyl-type proteinase., Comellas-Bigler M, Fuentes-Prior P, Maskos K, Huber R, Oyama H, Uchida K, Dunn BM, Oda K, Bode W, Structure. 2002 Jun;10(6):865-76. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12057200 12057200]
</div>
[[Category: Bacillus sp. mn-32]]
<div class="pdbe-citations 1gt9" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Bode, W.]]
<references/>
[[Category: Comellas-Bigler, M.]]
__TOC__
[[Category: Dunn, B.M.]]
</StructureSection>
[[Category: Fuentes-Prior, P.]]
[[Category: Bacillus subtilis]]
[[Category: Huber, R.]]
[[Category: Large Structures]]
[[Category: Maskos, K.]]
[[Category: Bode W]]
[[Category: Oda, K.]]
[[Category: Comellas-Bigler M]]
[[Category: Oyama, H.]]
[[Category: Dunn BM]]
[[Category: Uchida, K.]]
[[Category: Fuentes-Prior P]]
[[Category: CA]]
[[Category: Huber R]]
[[Category: SO4]]
[[Category: Maskos K]]
[[Category: serine-carboxyl type proteinase]]
[[Category: Oda K]]
[[Category: thermostable]]
[[Category: Oyama H]]
 
[[Category: Uchida K]]
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Retrieved from "https://proteopedia.org/1gt9"