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3tj9

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==Crystal structure of Helicobacter pylori UreE bound to Zn2+==
==Crystal structure of Helicobacter pylori UreE bound to Zn2+==
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<StructureSection load='3tj9' size='340' side='right' caption='[[3tj9]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
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<StructureSection load='3tj9' size='340' side='right'caption='[[3tj9]], [[Resolution|resolution]] 2.52&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tj9]] 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=3TJ9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TJ9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tj9]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TJ9 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.521&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tj8|3tj8]], [[3tja|3tja]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ureE, HP_0070 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tj9 OCA], [https://pdbe.org/3tj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tj9 RCSB], [https://www.ebi.ac.uk/pdbsum/3tj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tj9 ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tj9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tj9 RCSB], [http://www.ebi.ac.uk/pdbsum/3tj9 PDBsum]</span></td></tr>
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</table>
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<table>
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== Function ==
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<div style="background-color:#fffaf0;">
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[https://www.uniprot.org/uniprot/UREE_HELPY UREE_HELPY] Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly (By similarity).
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== Publication Abstract from PubMed ==
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The survival and growth of the pathogen Helicobacter pylori in the gastric acidic environment is ensured by the activity of urease, an enzyme containing two essential Ni2+ ions in the active site. The metallo-chaperone UreE facilitates in vivo Ni2+ insertion into the apo-enzyme. Crystals of apo-HpUreE and its Ni2+ and Zn2+ bound forms were obtained from protein solutions in the absence and presence of the metal ions. The crystal structures of the homodimeric protein, determined at 2.00 A (apo), 1.59 A (Ni) and 2.52 A (Zn) resolution, show the conserved proximal and solvent-exposed His102 residues from two adjacent monomers invariably involved in metal binding. The C-terminal regions of the apo-protein are disordered in the crystal, but acquire significant ordering in the presence of the metal ions due to the binding of His152. The analysis of X-ray absorption spectral data obtained on solutions of Ni2+- and Zn2+-HpUreE provided accurate information of the metal ion environment in the absence of solid-state effects. These results reveal the role of the histidine residues at the protein C-terminus in metal ion binding, and the mutual influence of protein framework and metal ion stereo-electronic properties in establishing coordination number and geometry leading to metal selectivity.
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Crystallographic and X-ray absorption spectroscopic characterization of Helicobacter pylori UreE bound to Ni2+ and Zn2+ reveal a role for the disordered C-terminal arm in metal trafficking.,Banaszak K, Martin-Diaconescu V, Bellucci M, Zambelli B, Rypniewski W, Maroney MJ, Ciurli S Biochem J. 2011 Oct 20. PMID:22010876<ref>PMID:22010876</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Urease accessory protein|Urease accessory protein]]
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Helicobacter pylori]]
[[Category: Helicobacter pylori]]
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[[Category: Banaszak, K.]]
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[[Category: Large Structures]]
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[[Category: Bellucci, M.]]
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[[Category: Banaszak K]]
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[[Category: Ciurli, S.]]
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[[Category: Bellucci M]]
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[[Category: Rypniewski, W R.]]
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[[Category: Ciurli S]]
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[[Category: Zambelli, B.]]
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[[Category: Rypniewski WR]]
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[[Category: Metal binding protein]]
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[[Category: Zambelli B]]
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[[Category: Urease accessory protein]]
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Current revision

Crystal structure of Helicobacter pylori UreE bound to Zn2+

PDB ID 3tj9

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