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[[Image:1gtj.gif|left|200px]]<br />
<applet load="1gtj" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gtj, resolution 1.75&Aring;" />
'''CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLISIN (KSCP)- COMPLEX WITH AC-ILE-ALA-PHE-CHO'''<br />


==Overview==
==Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Ala-Phe-cho==
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.
<StructureSection load='1gtj' size='340' side='right'caption='[[1gtj]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gtj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._MN-32 Bacillus sp. MN-32] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GTJ 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PHL:L-PHENYLALANINOL'>PHL</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=1gtj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtj OCA], [https://pdbe.org/1gtj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gtj RCSB], [https://www.ebi.ac.uk/pdbsum/1gtj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gtj 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/1gtj_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=1gtj 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>
1GTJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria] with SO4, CA and ACE as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GTJ 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: Bacteria]]
<div class="pdbe-citations 1gtj" 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 sp. MN-32]]
[[Category: Huber, R.]]
[[Category: Large Structures]]
[[Category: Maskos, K.]]
[[Category: Synthetic construct]]
[[Category: Oda, K.]]
[[Category: Bode W]]
[[Category: Oyama, H.]]
[[Category: Comellas-Bigler M]]
[[Category: Uchida, K.]]
[[Category: Dunn BM]]
[[Category: ACE]]
[[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]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov  5 16:19:01 2007''

Latest revision as of 12:05, 13 December 2023

Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Ala-Phe-cho

1gtj, resolution 1.75Å

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