This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1gtg
From Proteopedia
(Difference between revisions)
| (20 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1gtg.gif|left|200px]]<br /> | ||
| - | <applet load="1gtg" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1gtg, resolution 2.3Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF THE THERMOSTABLE SERINE-CARBOXYL TYPE PROTEINASE, KUMAMOLYSIN'''<br /> | ||
| - | == | + | ==Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp)== |
| - | Kumamolysin is a thermostable endopeptidase from Bacillus novosp. MN-32, exhibiting maximal proteolytic activity around pH 3. It belongs to the | + | <StructureSection load='1gtg' size='340' side='right'caption='[[1gtg]], [[Resolution|resolution]] 2.30Å' scene=''> |
| + | == Structural highlights == | ||
| + | <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> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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> | ||
| + | <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> | ||
| + | </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/1gtg_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=1gtg 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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: Bacillus sp. | + | <div class="pdbe-citations 1gtg" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Bode | + | <references/> |
| - | [[Category: Comellas-Bigler | + | __TOC__ |
| - | [[Category: Dunn | + | </StructureSection> |
| - | [[Category: Fuentes-Prior | + | [[Category: Bacillus sp. MN-32]] |
| - | [[Category: Huber | + | [[Category: Large Structures]] |
| - | [[Category: Maskos | + | [[Category: Bode W]] |
| - | [[Category: Oda | + | [[Category: Comellas-Bigler M]] |
| - | [[Category: Oyama | + | [[Category: Dunn BM]] |
| - | [[Category: Uchida | + | [[Category: Fuentes-Prior P]] |
| - | + | [[Category: Huber R]] | |
| - | + | [[Category: Maskos K]] | |
| - | + | [[Category: Oda K]] | |
| - | + | [[Category: Oyama H]] | |
| - | + | [[Category: Uchida K]] | |
Current revision
Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolysin (kscp)
| |||||||||||
Categories: Bacillus sp. MN-32 | Large Structures | Bode W | Comellas-Bigler M | Dunn BM | Fuentes-Prior P | Huber R | Maskos K | Oda K | Oyama H | Uchida K
