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| - | [[Image:2clb.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2clb| PDB=2clb | SCENE= }} | | {{STRUCTURE_2clb| PDB=2clb | SCENE= }} |
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| - | '''THE STRUCTURE OF THE DPS-LIKE PROTEIN FROM SULFOLOBUS SOLFATARICUS REVEALS A BACTERIOFERRITIN-LIKE DI-METAL BINDING SITE WITHIN A DPS-LIKE DODECAMERIC ASSEMBLY'''
| + | ===THE STRUCTURE OF THE DPS-LIKE PROTEIN FROM SULFOLOBUS SOLFATARICUS REVEALS A BACTERIOFERRITIN-LIKE DI-METAL BINDING SITE WITHIN A DPS-LIKE DODECAMERIC ASSEMBLY=== |
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| - | ==Overview==
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| - | The superfamily of ferritin-like proteins has recently expanded to include a phylogenetically distinct class of proteins termed DPS-like (DPSL) proteins. Despite their distinct genetic signatures, members of this subclass share considerable similarity to previously recognized DPS proteins. Like DPS, these proteins are expressed in response to oxidative stress, form dodecameric cage-like particles, preferentially utilize H(2)O(2) in the controlled oxidation of Fe(2+), and possess a short N-terminal extension implicated in stabilizing cellular DNA. Given these extensive similarities, the functional properties responsible for the preservation of the DPSL signature in the genomes of diverse prokaryotes have been unclear. Here, we describe the crystal structure of a DPSL protein from the thermoacidophilic archaeon Sulfolobus solfataricus. Although the overall fold of the polypeptide chain and the oligomeric state of this protein are indistinguishable from those of authentic DPS proteins, several important differences are observed. First, rather than a ferroxidase site at the subunit interface, as is observed in all other DPS proteins, the ferroxidase site in SsDPSL is buried within the four-helix bundle, similar to bacterioferritin. Second, the structure reveals a channel leading from the exterior surface of SsDPSL to the bacterioferritin-like dimetal binding site, possibly allowing divalent cations and/or H(2)O(2) to access the active site. Third, a pair of cysteine residues unique to DPSL proteins is found adjacent to the dimetal binding site juxtaposed between the exterior surface of the protein and the active site channel. The cysteine residues in this thioferritin motif may play a redox active role, possibly serving to recycle iron at the ferroxidase center. | + | The line below this paragraph, {{ABSTRACT_PUBMED_16953567}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16953567 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16953567}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Metal binding protein]] | | [[Category: Metal binding protein]] |
| | [[Category: Oxidative stress]] | | [[Category: Oxidative stress]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:25:03 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:12:56 2008'' |
Revision as of 09:13, 28 July 2008
Template:STRUCTURE 2clb
THE STRUCTURE OF THE DPS-LIKE PROTEIN FROM SULFOLOBUS SOLFATARICUS REVEALS A BACTERIOFERRITIN-LIKE DI-METAL BINDING SITE WITHIN A DPS-LIKE DODECAMERIC ASSEMBLY
Template:ABSTRACT PUBMED 16953567
About this Structure
2CLB is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly., Gauss GH, Benas P, Wiedenheft B, Young M, Douglas T, Lawrence CM, Biochemistry. 2006 Sep 12;45(36):10815-27. PMID:16953567
Page seeded by OCA on Mon Jul 28 12:12:56 2008
