1t1e: Difference between revisions

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New page: left|200px<br /><applet load="1t1e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t1e, resolution 1.18Å" /> '''High Resolution Crys...
 
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[[Image:1t1e.jpg|left|200px]]<br /><applet load="1t1e" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1t1e, resolution 1.18&Aring;" />
'''High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)'''<br />


==Overview==
==High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)==
Kumamolisin, an extracellular proteinase derived from an, acido/thermophilic Bacillus, belongs to the sedolisin family of, endopeptidases characterized by a subtilisin-like fold and a Ser-Glu-Asp, catalytic triad. In kumamolisin, the Asp82 carboxylate hydrogen bonds to, Glu32-Trp129, which might act as a proton sink stabilizing the catalytic, residues. The 1.2/1.3 A crystal structures of the Glu32--&gt;Ala and, Trp129--&gt;Ala mutants show that both mutations affect the active-site, conformation, causing a 95% activity decrease. In addition, the 1.2 A, crystal structure of the Ser278--&gt;Ala mutant of pro-kumamolisin was, determined. The prodomain exhibits a half-beta sandwich core docking to, the catalytic domain similarly as the equivalent subtilisin prodomains in, their catalytic-domain complexes. This pro-kumamolisin structure displays, for the first time, the uncleaved linker segment running across the active, site and connecting the prodomain with the properly folded catalytic, domain. The structure strongly points to an initial intramolecular, activation cleavage in subtilases, as presumed for pro-subtilisin and, pro-furin.
<StructureSection load='1t1e' size='340' side='right'caption='[[1t1e]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1t1e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._MN-32 Bacillus sp. MN-32]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T1E FirstGlance]. <br>
1T1E 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 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T1E OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.18&#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></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1e OCA], [https://pdbe.org/1t1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t1e RCSB], [https://www.ebi.ac.uk/pdbsum/1t1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t1e ProSAT]</span></td></tr>
1.2 A crystal structure of the serine carboxyl proteinase pro-kumamolisin; structure of an intact pro-subtilase., Comellas-Bigler M, Maskos K, Huber R, Oyama H, Oda K, Bode W, Structure. 2004 Jul;12(7):1313-23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15242607 15242607]
</table>
[[Category: Bacillus sp. mn-32]]
== Function ==
[[Category: Single protein]]
[https://www.uniprot.org/uniprot/Q8RR56_9BACI Q8RR56_9BACI]  
[[Category: Bode, W.]]
== Evolutionary Conservation ==
[[Category: Comellas-Bigler, M.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Huber, R.]]
Check<jmol>
[[Category: Maskos, K.]]
  <jmolCheckbox>
[[Category: Oda, K.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t1/1t1e_consurf.spt"</scriptWhenChecked>
[[Category: Oyama, H.]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: CA]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: activation mechanism]]
  </jmolCheckbox>
[[Category: proenzyme]]
</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=1t1e ConSurf].
[[Category: prosubtilase]]
<div style="clear:both"></div>
[[Category: sedolisin]]
__TOC__
[[Category: serine-carboxyl proteinase]]
</StructureSection>
 
[[Category: Bacillus sp. MN-32]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 01:28:06 2007''
[[Category: Large Structures]]
[[Category: Bode W]]
[[Category: Comellas-Bigler M]]
[[Category: Huber R]]
[[Category: Maskos K]]
[[Category: Oda K]]
[[Category: Oyama H]]

Latest revision as of 08:35, 14 February 2024

High Resolution Crystal Structure of the Intact Pro-Kumamolisin, a Sedolisin Type Proteinase (previously called Kumamolysin or KSCP)

1t1e, resolution 1.18Å

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