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4l3k

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Revision as of 09:08, 5 August 2016

Crystal structure of Sporosarcina pasteurii UreE bound to Ni2+ and Zn2+

Structural highlights

4l3k is a 2 chain structure with sequence from "urobacillus_pasteurii"_miquel_1889 "urobacillus pasteurii" miquel 1889. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Gene:	ureE ("Urobacillus pasteurii" Miquel 1889)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UREE_BACPA] Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.[HAMAP-Rule:MF_00822]

Publication Abstract from PubMed

Urease is a nickel-dependent enzyme that plays a critical role in the biogeochemical nitrogen cycle by catalyzing the hydrolysis of urea to ammonia and carbamate. This enzyme, initially synthesized in the apo form, needs to be activated by incorporation of two nickel ions into the active site, a process driven by the dimeric metallochaperone UreE. Previous studies reported that this protein can bind different metal ions in vitro, beside the cognate Ni(II). This study explores the metal selectivity and affinity of UreE from Sporosarcina pasteurii (Sp, formerly known as Bacillus pasteurii) for cognate [Ni(II)] and noncognate [Zn(II)] metal ions. In particular, the thermodynamic parameters of SpUreE Ni(II) and Zn(II) binding have been determined using isothermal titration calorimetry. These experiments show that two Ni(II) ions bind to the protein dimer with positive cooperativity. The high-affinity site involves the conserved solvent-exposed His(100) and the C-terminal His(145), whereas the low-affinity site comprises also the C-terminal His(147). Zn(II) binding to the protein, occurring in the same protein regions and with similar affinity as compared to Ni(II), causes metal-driven dimerization of the protein dimer. The crystal structure of the protein obtained in the presence of equimolar amounts of both metal ions indicates that the high-affinity metal binding site binds Ni(II) preferentially over Zn(II). The ability of the protein to select Ni(II) over Zn(II) was confirmed by competition experiments in solution as well as by analysis of X-ray anomalous dispersion data. Overall, the thermodynamics and structural parameters that modulate the metal ion specificity of the different binding sites on the protein surface of SpUreE have been established.

Selectivity of Ni(II) and Zn(II) binding to Sporosarcina pasteurii UreE, a metallochaperone in the urease assembly: a calorimetric and crystallographic study.,Zambelli B, Banaszak K, Merloni A, Kiliszek A, Rypniewski W, Ciurli S J Biol Inorg Chem. 2013 Dec;18(8):1005-17. doi: 10.1007/s00775-013-1049-6. Epub, 2013 Oct 15. PMID:24126709^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zambelli B, Banaszak K, Merloni A, Kiliszek A, Rypniewski W, Ciurli S. Selectivity of Ni(II) and Zn(II) binding to Sporosarcina pasteurii UreE, a metallochaperone in the urease assembly: a calorimetric and crystallographic study. J Biol Inorg Chem. 2013 Dec;18(8):1005-17. doi: 10.1007/s00775-013-1049-6. Epub, 2013 Oct 15. PMID:24126709 doi:http://dx.doi.org/10.1007/s00775-013-1049-6

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4l3k"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Sporosarcina pasteurii UreE bound to Ni2+ and Zn2+==
 <StructureSection load='4l3k' size='340' side='right' caption='[[4l3k]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ureE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1474 "Urobacillus pasteurii" Miquel 1889])</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=4l3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l3k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l3k RCSB], [http://www.ebi.ac.uk/pdbsum/4l3k PDBsum]</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=4l3k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l3k OCA], [http://pdbe.org/4l3k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l3k RCSB], [http://www.ebi.ac.uk/pdbsum/4l3k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l3k ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4l3k" style="background-color:#fffaf0;"></div>
 ==See Also==

4l3k

From Proteopedia

Revision as of 09:08, 5 August 2016

Crystal structure of Sporosarcina pasteurii UreE bound to Ni2+ and Zn2+

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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