5g4h
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==1.50 A resolution catechol (1,2-dihydroxybenzene) inhibited Sporosarcina pasteurii urease== | |
| + | <StructureSection load='5g4h' size='340' side='right' caption='[[5g4h]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5g4h]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Sporosarcina_pasteurii Sporosarcina pasteurii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G4H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5G4H FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAQ:CATECHOL'>CAQ</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CXM:N-CARBOXYMETHIONINE'>CXM</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Urease Urease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.5 3.5.1.5] </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=5g4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g4h OCA], [http://pdbe.org/5g4h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5g4h RCSB], [http://www.ebi.ac.uk/pdbsum/5g4h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5g4h ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Urease is a Ni(II)-containing enzyme that catalyzes the hydrolysis of urea to yield ammonia and carbamate at a rate 1015 times higher than the uncatalyzed reaction. Urease is a virulence factor of several human pathogens, in addition to decreasing the efficiency of soil organic nitrogen fertilization. Therefore, efficient urease inhibitors are actively sought. In this study, we describe a molecular characterization of the interaction between urease from Sporosarcina pasteurii (SPU) and Canavalia ensiformis (jack bean, JBU) with catechol, a model polyphenol. In particular, catechol irreversibly inactivates both SPU and JBU with a complex radical-based autocatalytic multistep mechanism. The crystal structure of the SPU-catechol complex, determined at 1.50A resolution, reveals the structural details of the enzyme inhibition. | ||
| - | + | Inactivation of urease by catechol: Kinetics and structure.,Mazzei L, Cianci M, Musiani F, Lente G, Palombo M, Ciurli S J Inorg Biochem. 2016 Nov 9;166:182-189. doi: 10.1016/j.jinorgbio.2016.11.016. PMID:27888701<ref>PMID:27888701</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5g4h" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Sporosarcina pasteurii]] | ||
| + | [[Category: Urease]] | ||
| + | [[Category: Cianci, M]] | ||
| + | [[Category: Ciurli, S]] | ||
[[Category: Mazzei, L]] | [[Category: Mazzei, L]] | ||
[[Category: Musiani, F]] | [[Category: Musiani, F]] | ||
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | + | ||
Revision as of 19:37, 9 December 2016
1.50 A resolution catechol (1,2-dihydroxybenzene) inhibited Sporosarcina pasteurii urease
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