1gt9

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[[Image:1gt9.jpg|left|200px]]
 
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{{Structure
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==High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp)==
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|PDB= 1gt9 |SIZE=350|CAPTION= <scene name='initialview01'>1gt9</scene>, resolution 1.38&Aring;
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<StructureSection load='1gt9' size='340' side='right'caption='[[1gt9]], [[Resolution|resolution]] 1.38&Aring;' scene=''>
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|SITE= <scene name='pdbsite=CA1:Ca+Binding+Site+For+Chain+2'>CA1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<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>
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|ACTIVITY=
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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]] 1.38&#8491;</td></tr>
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|GENE=
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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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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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=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>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gt9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gt9 OCA], [http://www.ebi.ac.uk/pdbsum/1gt9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gt9 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q8RR56_9BACI Q8RR56_9BACI]
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== Evolutionary Conservation ==
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'''HIGH RESOLUTION CRYSTAL STRUCTURE OF A THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE'''
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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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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gt/1gt9_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=1gt9 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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1GT9 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=1GT9 OCA].
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==Reference==
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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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[[Category: Bacteria]]
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[[Category: Single protein]]
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[[Category: Bode, W.]]
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[[Category: Comellas-Bigler, M.]]
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[[Category: Dunn, B M.]]
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[[Category: Fuentes-Prior, P.]]
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[[Category: Huber, R.]]
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[[Category: Maskos, K.]]
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[[Category: Oda, K.]]
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[[Category: Oyama, H.]]
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[[Category: Uchida, K.]]
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[[Category: serine-carboxyl type proteinase]]
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[[Category: thermostable]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:50:55 2008''
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1gt9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus subtilis]]
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[[Category: Large Structures]]
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[[Category: Bode W]]
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[[Category: Comellas-Bigler M]]
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[[Category: Dunn BM]]
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[[Category: Fuentes-Prior P]]
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[[Category: Huber R]]
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[[Category: Maskos K]]
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[[Category: Oda K]]
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[[Category: Oyama H]]
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[[Category: Uchida K]]

Current revision

High resolution crystal structure of a thermostable serine-carboxyl type proteinase, kumamolisin (kscp)

PDB ID 1gt9

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