3dyb
From Proteopedia
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- | [[ | + | ==proteinase K- digalacturonic acid complex== |
+ | <StructureSection load='3dyb' size='340' side='right' caption='[[3dyb]], [[Resolution|resolution]] 1.32Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3dyb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Engyodontium_album Engyodontium album]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DYB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DYB FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AD0:DIGALACTURONIC+ACID'>AD0</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidase_K Peptidase K], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.64 3.4.21.64] </span></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dyb RCSB], [http://www.ebi.ac.uk/pdbsum/3dyb PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == 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/dy/3dyb_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> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Proteinase K, a subtilisin-like fungal protease, was crystallized from a cocktail of small molecules containing digalacturonic acid (DGA). The crystal structure was determined to 1.32 A resolution and refined to an R factor of 0.158. The final model contained, beside the protein, two calcium ions, 379 water molecules, a molecule of DGA and a partially occupied HEPES molecule. The DGA molecule has one sugar moiety disposed exactly on a crystallographic twofold axis; the second ring was not observed. The DGA molecule is bound to two protein molecules across the twofold axis through hydrogen-bonding networks involving Ser150 and water molecules. One of the calcium-ion sites has not been reported previously. This study further illustrates the involvement of small molecules in the crystallization of macromolecules through their ability to form intermolecular lattice interactions. | ||
- | + | High-resolution structure of proteinase K cocrystallized with digalacturonic acid.,Larson SB, Day JS, Nguyen C, Cudney R, McPherson A Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Mar 1;65(Pt, 3):192-8. Epub 2009 Feb 12. PMID:19255463<ref>PMID:19255463</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
- | + | ==See Also== | |
- | + | *[[Proteinase|Proteinase]] | |
- | == | + | == References == |
- | [[ | + | <references/> |
- | + | __TOC__ | |
- | == | + | </StructureSection> |
- | < | + | |
[[Category: Engyodontium album]] | [[Category: Engyodontium album]] | ||
[[Category: Peptidase K]] | [[Category: Peptidase K]] | ||
- | [[Category: CHTSB, Center for High-Throughput Structural Biology | + | [[Category: CHTSB, Center for High-Throughput Structural Biology]] |
- | [[Category: Cudney, R | + | [[Category: Cudney, R]] |
- | [[Category: Day, J S | + | [[Category: Day, J S]] |
- | [[Category: Larson, S B | + | [[Category: Larson, S B]] |
- | [[Category: McPherson, A | + | [[Category: McPherson, A]] |
- | [[Category: Nguyen, C | + | [[Category: Nguyen, C]] |
[[Category: Center for high-throughput structural biology]] | [[Category: Center for high-throughput structural biology]] | ||
[[Category: Chtsb]] | [[Category: Chtsb]] | ||
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[[Category: Porteinase k]] | [[Category: Porteinase k]] | ||
[[Category: Protease]] | [[Category: Protease]] | ||
- | [[Category: Protein structure initiative | + | [[Category: PSI, Protein structure initiative]] |
- | + | ||
[[Category: Serine protease]] | [[Category: Serine protease]] | ||
[[Category: Silverbullet]] | [[Category: Silverbullet]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
[[Category: Zymogen]] | [[Category: Zymogen]] |
Revision as of 13:22, 19 November 2014
proteinase K- digalacturonic acid complex
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Categories: Engyodontium album | Peptidase K | CHTSB, Center for High-Throughput Structural Biology | Cudney, R | Day, J S | Larson, S B | McPherson, A | Nguyen, C | Center for high-throughput structural biology | Chtsb | Digalacturonic acid | Hepe | Hydrolase | Metal-binding | Porteinase k | Protease | PSI, Protein structure initiative | Serine protease | Silverbullet | Structural genomic | Zymogen