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1eb0

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Crystal structure of Bacillus pasteurii UreE at 1.85 A, phased by SIRAS. Type I crystal form.

Structural highlights

1eb0 is a 1 chain structure with sequence from Sporosarcina pasteurii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UREE_SPOPA Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.

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 PubMed

Bacillus pasteurii UreE (BpUreE) is a putative chaperone assisting the insertion of Ni(2+) ions in the active site of urease. The x-ray structure of the protein has been determined for two crystal forms, at 1.7 and 1.85 A resolution, using SIRAS phases derived from a Hg(2+)-derivative. BpUreE is composed of distinct N- and C-terminal domains, connected by a short flexible linker. The structure reveals the topology of an elongated homodimer, formed by interaction of the two C-terminal domains through hydrophobic interactions. A single Zn(2+) ion bound to four conserved His-100 residues, one from each monomer, connects two dimers resulting in a tetrameric BpUreE known to be formed in concentrated solutions. The Zn(2+) ion can be replaced by Ni(2+) as shown by anomalous difference maps obtained on a crystal of BpUreE soaked in a solution containing NiCl(2). A large hydrophobic patch surrounding the metal ion site is surface-exposed in the biologically relevant dimer. The BpUreE structure represents the first for this class of proteins and suggests a possible role for UreE in the urease nickel-center assembly.

Structural basis for Ni(2+) transport and assembly of the urease active site by the metallochaperone UreE from Bacillus pasteurii.,Remaut H, Safarov N, Ciurli S, Van Beeumen J J Biol Chem. 2001 Dec 28;276(52):49365-70. Epub 2001 Oct 15. PMID:11602602^[1]

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

References

↑ Remaut H, Safarov N, Ciurli S, Van Beeumen J. Structural basis for Ni(2+) transport and assembly of the urease active site by the metallochaperone UreE from Bacillus pasteurii. J Biol Chem. 2001 Dec 28;276(52):49365-70. Epub 2001 Oct 15. PMID:11602602 doi:10.1074/jbc.M108304200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1eb0"

@@ Line 3: / Line 3: @@
 <StructureSection load='1eb0' size='340' side='right'caption='[[1eb0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1eb0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"urobacillus_pasteurii"_miquel_1889 "urobacillus pasteurii" miquel 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EB0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1eb0]] is a 1 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=1EB0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EB0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.85&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ear|1ear]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1eb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb0 OCA], [https://pdbe.org/1eb0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1eb0 RCSB], [https://www.ebi.ac.uk/pdbsum/1eb0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1eb0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/UREE_BACPA UREE_BACPA]] Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.[HAMAP-Rule:MF_00822]
+[https://www.uniprot.org/uniprot/UREE_SPOPA UREE_SPOPA] Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Urease accessory protein|Urease accessory protein]]
+*[[Urease accessory protein 3D structures|Urease accessory protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Urobacillus pasteurii miquel 1889]]
 [[Category: Large Structures]]
-[[Category: Beeumen, J Van]]
+[[Category: Sporosarcina pasteurii]]
-[[Category: Ciurli, S]]
+[[Category: Ciurli S]]
-[[Category: Remaut, H]]
+[[Category: Remaut H]]
-[[Category: Safarov, N]]
+[[Category: Safarov N]]
-[[Category: Chaperone]]
+[[Category: Van Beeumen J]]
-[[Category: Putative ni-chaperone]]
-[[Category: Urease accessory protein]]

1eb0

From Proteopedia

Current revision

Crystal structure of Bacillus pasteurii UreE at 1.85 A, phased by SIRAS. Type I crystal form.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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