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1gtg

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[[Image:1gtg.gif|left|200px]]
 
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==Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp)==
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The line below this paragraph, containing "STRUCTURE_1gtg", creates the "Structure Box" on the page.
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<StructureSection load='1gtg' size='340' side='right'caption='[[1gtg]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1gtg]] 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=1GTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GTG FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_1gtg| PDB=1gtg | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gtg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtg OCA], [https://pdbe.org/1gtg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gtg RCSB], [https://www.ebi.ac.uk/pdbsum/1gtg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gtg ProSAT]</span></td></tr>
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</table>
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'''CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLYSIN'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q8RR56_9BACI Q8RR56_9BACI]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gt/1gtg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1gtg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== 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.
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.
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==About this Structure==
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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>
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1GTG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacteria Bacteria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTG OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://www.ncbi.nlm.nih.gov/pubmed/12057200 12057200]
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</div>
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[[Category: Bacteria]]
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<div class="pdbe-citations 1gtg" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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== References ==
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[[Category: Bode, W.]]
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<references/>
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[[Category: Comellas-Bigler, M.]]
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__TOC__
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[[Category: Dunn, B M.]]
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</StructureSection>
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[[Category: Fuentes-Prior, P.]]
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[[Category: Bacillus sp. MN-32]]
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[[Category: Huber, R.]]
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[[Category: Large Structures]]
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[[Category: Maskos, K.]]
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[[Category: Bode W]]
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[[Category: Oda, K.]]
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[[Category: Comellas-Bigler M]]
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[[Category: Oyama, H.]]
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[[Category: Dunn BM]]
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[[Category: Uchida, K.]]
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[[Category: Fuentes-Prior P]]
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[[Category: Serine-carboxyl type proteinase]]
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[[Category: Huber R]]
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[[Category: Thermostable]]
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[[Category: Maskos K]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:59:10 2008''
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[[Category: Oda K]]
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[[Category: Oyama H]]
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[[Category: Uchida K]]

Current revision

Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp)

PDB ID 1gtg

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