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| - | [[Image:1se8.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1se8| PDB=1se8 | SCENE= }} | | {{STRUCTURE_1se8| PDB=1se8 | SCENE= }} |
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| - | '''Structure of single-stranded DNA-binding protein (SSB) from D. radiodurans'''
| + | ===Structure of single-stranded DNA-binding protein (SSB) from D. radiodurans=== |
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| - | ==Overview==
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| - | Single-stranded DNA (ssDNA)-binding (SSB) proteins are uniformly required to bind and protect single-stranded intermediates in DNA metabolic pathways. All bacterial and eukaryotic SSB proteins studied to date oligomerize to assemble four copies of a conserved domain, called an oligonucleotide/oligosaccharide-binding (OB) fold, that cooperate in nonspecific ssDNA binding. The vast majority of bacterial SSB family members function as homotetramers, with each monomer contributing a single OB fold. However, SSB proteins from the Deinococcus-Thermus genera are exceptions to this rule, because they contain two OB folds per monomer. To investigate the structural consequences of this unusual arrangement, we have determined a 1.8-A-resolution x-ray structure of Deinococcus radiodurans SSB. The structure shows that D. radiodurans SSB comprises two OB domains linked by a beta-hairpin motif. The protein assembles a four-OB-fold arrangement by means of symmetric dimerization. In contrast to homotetrameric SSB proteins, asymmetry exists between the two OB folds of D. radiodurans SSB because of sequence differences between the domains. These differences appear to reflect specialized roles that have evolved for each domain. Extensive crystallographic contacts link D. radiodurans SSB dimers in an arrangement that has important implications for higher-order structures of the protein bound to ssDNA. This assembly utilizes the N-terminal OB domain and the beta-hairpin structure that is unique to Deinococcus and Thermus species SSB proteins. We hypothesize that differences between D. radiodurans SSB and homotetrameric bacterial SSB proteins may confer a selective advantage to D. radiodurans cells that aids viability in environments that challenge genomic stability.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15159541}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15159541 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15159541}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Misic, A M.]] | | [[Category: Misic, A M.]] |
| | [[Category: Single-strand binding protein]] | | [[Category: Single-strand binding protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:35:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:55:13 2008'' |
Revision as of 17:55, 28 July 2008
Template:STRUCTURE 1se8
Structure of single-stranded DNA-binding protein (SSB) from D. radiodurans
Template:ABSTRACT PUBMED 15159541
About this Structure
1SE8 is a Single protein structure of sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA.
Reference
Crystal structure of the Deinococcus radiodurans single-stranded DNA-binding protein suggests a mechanism for coping with DNA damage., Bernstein DA, Eggington JM, Killoran MP, Misic AM, Cox MM, Keck JL, Proc Natl Acad Sci U S A. 2004 Jun 8;101(23):8575-80. Epub 2004 May 24. PMID:15159541
Page seeded by OCA on Mon Jul 28 20:55:13 2008
