5g4h: Difference between revisions
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==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=5G4H 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]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAQ:CATECHOL'>CAQ</scene>, <scene name='pdbligand=CXM:N-CARBOXYMETHIONINE'>CXM</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5g4h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g4h OCA], [https://pdbe.org/5g4h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g4h RCSB], [https://www.ebi.ac.uk/pdbsum/5g4h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g4h ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/URE3_SPOPA URE3_SPOPA] | |||
<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> | ||
[[Category: | <div class="pdbe-citations 5g4h" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Ciurli | ==See Also== | ||
[[Category: | *[[Urease 3D structures|Urease 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sporosarcina pasteurii]] | |||
[[Category: Cianci M]] | |||
[[Category: Ciurli S]] | |||
[[Category: Mazzei L]] | |||
[[Category: Musiani F]] | |||
Latest revision as of 16:38, 26 July 2023
1.50 A resolution catechol (1,2-dihydroxybenzene) inhibited Sporosarcina pasteurii urease1.50 A resolution catechol (1,2-dihydroxybenzene) inhibited Sporosarcina pasteurii urease
Structural highlights
FunctionPublication Abstract from PubMedUrease 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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