3la0: Difference between revisions
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==Crystal Structure of UreE from Helicobacter pylori (metal of unknown identity bound)== | |||
<StructureSection load='3la0' size='340' side='right' caption='[[3la0]], [[Resolution|resolution]] 2.86Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3la0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LA0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l9z|3l9z]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_0070, ureE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])</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=3la0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3la0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3la0 RCSB], [http://www.ebi.ac.uk/pdbsum/3la0 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/la/3la0_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 == | |||
The crystal structure of the urease maturation protein UreE from Helicobacter pylori has been determined in its apo form at 2.1 A resolution, bound to Cu(2+) at 2.7 A resolution, and bound to Ni(2+) at 3.1 A resolution. Apo UreE forms dimers, while the metal-bound enzymes are arranged as tetramers that consist of a dimer of dimers associated around the metal ion through coordination by His102 residues from each subunit of the tetramer. Comparison of independent subunits from different crystal forms indicates changes in the relative arrangement of the N- and C-terminal domains in response to metal binding. The improved ability of engineered versions of UreE containing hexahistidine sequences at either the N-terminal or C-terminal end to provide Ni(2+) for the final metal sink (urease) is eliminated in the H102A version. Therefore, the ability of the improved Ni(2+)-binding versions to deliver more nickel is likely an effect of an increased local concentration of metal ions that can rapidly replenish transferred ions bound to His102. | |||
Crystal Structures of Apo and Metal-Bound Forms of the UreE Protein from Helicobacter pylori: Role of Multiple Metal Binding Sites .,Shi R, Munger C, Asinas A, Benoit SL, Miller E, Matte A, Maier RJ, Cygler M Biochemistry. 2010 Aug 24;49(33):7080-8. PMID:20681615<ref>PMID:20681615</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== | ==See Also== | ||
*[[Urease accessory protein|Urease accessory protein]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Assinas, A | [[Category: Assinas, A]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Cygler, M | [[Category: Cygler, M]] | ||
[[Category: Matte, A | [[Category: Matte, A]] | ||
[[Category: Munger, C | [[Category: Munger, C]] | ||
[[Category: Shi, R | [[Category: Shi, R]] | ||
[[Category: Bsgi]] | [[Category: Bsgi]] | ||
[[Category: Chaperone]] | [[Category: Chaperone]] | ||
[[Category: Metal binding protein]] | [[Category: Metal binding protein]] | ||
[[Category: Nickel]] | [[Category: Nickel]] | ||
[[Category: Nickel insertion]] | [[Category: Nickel insertion]] | ||
[[Category: Uree in metal-bound form]] | [[Category: Uree in metal-bound form]] | ||
[[Category: Virulence]] | [[Category: Virulence]] | ||
Revision as of 18:18, 18 December 2014
Crystal Structure of UreE from Helicobacter pylori (metal of unknown identity bound)Crystal Structure of UreE from Helicobacter pylori (metal of unknown identity bound)
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of the urease maturation protein UreE from Helicobacter pylori has been determined in its apo form at 2.1 A resolution, bound to Cu(2+) at 2.7 A resolution, and bound to Ni(2+) at 3.1 A resolution. Apo UreE forms dimers, while the metal-bound enzymes are arranged as tetramers that consist of a dimer of dimers associated around the metal ion through coordination by His102 residues from each subunit of the tetramer. Comparison of independent subunits from different crystal forms indicates changes in the relative arrangement of the N- and C-terminal domains in response to metal binding. The improved ability of engineered versions of UreE containing hexahistidine sequences at either the N-terminal or C-terminal end to provide Ni(2+) for the final metal sink (urease) is eliminated in the H102A version. Therefore, the ability of the improved Ni(2+)-binding versions to deliver more nickel is likely an effect of an increased local concentration of metal ions that can rapidly replenish transferred ions bound to His102. Crystal Structures of Apo and Metal-Bound Forms of the UreE Protein from Helicobacter pylori: Role of Multiple Metal Binding Sites .,Shi R, Munger C, Asinas A, Benoit SL, Miller E, Matte A, Maier RJ, Cygler M Biochemistry. 2010 Aug 24;49(33):7080-8. PMID:20681615[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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