1eb0
From Proteopedia
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|PDB= 1eb0 |SIZE=350|CAPTION= <scene name='initialview01'>1eb0</scene>, resolution 1.85Å | |PDB= 1eb0 |SIZE=350|CAPTION= <scene name='initialview01'>1eb0</scene>, resolution 1.85Å | ||
|SITE= <scene name='pdbsite=ZN:Zn+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+Co+...'>ZN</scene> | |SITE= <scene name='pdbsite=ZN:Zn+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+Co+...'>ZN</scene> | ||
- | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1eb0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eb0 OCA], [http://www.ebi.ac.uk/pdbsum/1eb0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1eb0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Remaut, H.]] | [[Category: Remaut, H.]] | ||
[[Category: Safarov, N.]] | [[Category: Safarov, N.]] | ||
- | [[Category: ZN]] | ||
[[Category: putative ni-chaperone]] | [[Category: putative ni-chaperone]] | ||
[[Category: urease accessory protein]] | [[Category: urease accessory protein]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:59:02 2008'' |
Revision as of 16:59, 30 March 2008
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, resolution 1.85Å | |||||||
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Ligands: | |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF BACILLUS PASTEURII UREE AT 1.85 A, PHASED BY SIRAS. TYPE I 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
1EB0 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
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