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1gtj
From Proteopedia
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| - | [[Image: | + | ==Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Ala-Phe-cho== |
| + | <StructureSection load='1gtj' size='340' side='right' caption='[[1gtj]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | [[1gtj]] is a 4 chain structure with sequence from [http://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=1GTJ OCA]. <br> | ||
| + | <b>Related:</b> [[1gt9|1gt9]], [[1gtg|1gtg]], [[1gtl|1gtl]]<br> | ||
| + | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | == 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> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Bacillus sp. mn-32]] | |
| - | + | ||
| - | == | + | |
| - | < | + | |
| - | [[Category: | + | |
[[Category: Bode, W.]] | [[Category: Bode, W.]] | ||
[[Category: Comellas-Bigler, M.]] | [[Category: Comellas-Bigler, M.]] | ||
Revision as of 08:28, 30 April 2014
Crystal structure of the thermostable serine-carboxyl type proteinase, kumamolisin (KSCP) - complex with Ac-Ile-Ala-Phe-cho
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