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==3.0 A Model of Iron Containing Urease UreA2B2 from Helicobacter mustelae (refined w/ no ordered solvent)==
==3.0 A Model of Iron Containing Urease UreA2B2 from Helicobacter mustelae (refined w/ no ordered solvent)==
<StructureSection load='3qgk' size='340' side='right' caption='[[3qgk]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='3qgk' size='340' side='right'caption='[[3qgk]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qgk]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_mustelae Helicobacter mustelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QGK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QGK FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qgk]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_mustelae_12198 Helicobacter mustelae 12198]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QGK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3qga|3qga]]</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=3qgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qgk OCA], [https://pdbe.org/3qgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qgk RCSB], [https://www.ebi.ac.uk/pdbsum/3qgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qgk ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HMU13020, ureA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=217 Helicobacter mustelae]), HMU13010, ureB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=217 Helicobacter mustelae])</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=3qgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qgk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qgk RCSB], [http://www.ebi.ac.uk/pdbsum/3qgk PDBsum]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/D3UJ81_HELM1 D3UJ81_HELM1]
Helicobacter mustelae, a gastric pathogen of ferrets, synthesizes a distinct iron-dependent urease in addition to its archetypical nickel-containing enzyme. The iron-urease is oxygen-labile, with the inactive protein exhibiting a methemerythrin-like electronic spectrum. Significantly, incubation of the oxidized protein with dithionite under anaerobic conditions leads to restoration of activity and bleaching of the spectrum. Structural analysis of the oxidized species reveals a dinuclear iron metallocenter bridged by a lysine carbamate, closely resembling the traditional nickel-urease active site. Although the iron-urease is less active than the nickel-enzyme, its activity allows H. mustelae to survive the carnivore's low-nickel gastric environment.
 
Iron-containing urease in a pathogenic bacterium.,Carter EL, Tronrud DE, Taber SR, Karplus PA, Hausinger RP Proc Natl Acad Sci U S A. 2011 Jul 25. PMID:21788478<ref>PMID:21788478</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Urease|Urease]]
*[[Urease 3D structures|Urease 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Helicobacter mustelae]]
[[Category: Helicobacter mustelae 12198]]
[[Category: Urease]]
[[Category: Large Structures]]
[[Category: Karplus, P A]]
[[Category: Karplus PA]]
[[Category: Robbins, A]]
[[Category: Robbins A]]
[[Category: Tronrud, D E]]
[[Category: Tronrud DE]]
[[Category: Alpha-beta barrel]]
[[Category: Hydrolase]]
[[Category: Iron metalloenzyme]]
Retrieved from "https://proteopedia.org/3qgk"