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1ear

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[[Image:1ear.gif|left|200px]]
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{{Structure
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|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+Co+...'>AC1</scene>
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{{STRUCTURE_1ear| PDB=1ear | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ear FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ear OCA], [http://www.ebi.ac.uk/pdbsum/1ear PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ear RCSB]</span>
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'''CRYSTAL STRUCTURE OF BACILLUS PASTEURII UREE AT 1.7 A. TYPE II CRYSTAL FORM.'''
'''CRYSTAL STRUCTURE OF BACILLUS PASTEURII UREE AT 1.7 A. TYPE II CRYSTAL FORM.'''
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[[Category: Remaut, H.]]
[[Category: Remaut, H.]]
[[Category: Safarov, N.]]
[[Category: Safarov, N.]]
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[[Category: putative ni-chaperone]]
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[[Category: Putative ni-chaperone]]
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[[Category: urease operon]]
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[[Category: Urease operon]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:52:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:58:53 2008''
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Revision as of 11:52, 2 May 2008

Template:STRUCTURE 1ear

CRYSTAL STRUCTURE OF BACILLUS PASTEURII UREE AT 1.7 A. TYPE II CRYSTAL FORM.


Overview

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.

About this Structure

1EAR is a Single protein structure of sequence from Sporosarcina pasteurii. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 14:52:47 2008

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