Single-stranded DNA-binding protein

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'''Single-stranded DNA-binding protein''' (SSB) binds to single-stranded regions of DNA (ssDNA) to protect it from annealing, prevention of secondary structure formation and digestion. SSB binds to DNA in a sequence-independent manner. The binding of SSB enables processes like replication, DNA repair and recombination to occur. SSB can form complexes with specific genome maintenance proteins helping their activities. See also [[Single stranded binding protein]].
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'''Single-stranded DNA-binding protein''' (SSB) binds to single-stranded regions of DNA (ssDNA) to protect it from annealing, prevention of secondary structure formation and digestion. SSB binds to DNA in a sequence-independent manner. The binding of SSB enables processes like replication, DNA repair and recombination to occur. SSB can form complexes with specific genome maintenance proteins helping their activities. Viral SSB proteins are monomeric while eukaryotic SSB ('''Replication protein A''' – RPA) is a heterotrimer composed of RPA70, RPA32 and RPA14. RPA has 6 DNA-binding domains (DBD). The '''mitochondrial human SSB (HsmtSSB)''' is a homotetramer. See also [[Single stranded binding protein]].
== 3D Structures of single-stranded DNA-binding protein ==
== 3D Structures of single-stranded DNA-binding protein ==
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[[1urj]] – SSB – human herpesvirus 1 <br />
[[1urj]] – SSB – human herpesvirus 1 <br />
[[1pfs]] – SSB (mutant) – Pseudomonas phage PF3 - NMR<br />
[[1pfs]] – SSB (mutant) – Pseudomonas phage PF3 - NMR<br />
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[[3ull]], [[1s3o]], [[2dud]] – hSSB residues 16-148 – human <br />
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[[3ull]], [[1s3o]], [[2dud]] – HsmtSSB residues 16-148 – human <br />
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[[1fgu]] – hSSB central domain<br />
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[[2b29]] – hSSB N terminal domain<br />
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[[4ipc]], [[4ipd]], [[4ipg]] – hSSB N terminal domain (mutant)<br />
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[[1kaw]] – EcSSB chymotryptic domain – ''Escherichia coli'' <br />
[[1kaw]] – EcSSB chymotryptic domain – ''Escherichia coli'' <br />
[[1qvc]], [[1sru]] – EcSSB <br />
[[1qvc]], [[1sru]] – EcSSB <br />
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[[3ufm]], [[3uf7]] – DrSSB C terminal + uracil-DNA glycosylase <br />
[[3ufm]], [[3uf7]] – DrSSB C terminal + uracil-DNA glycosylase <br />
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[[2b3g]] – hSSB N terminal domain + tumor suppressor P53<br />
 
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[[4nb3]] – hSSB N terminal domain (mutant) + polypeptide<br />
 
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[[4ijh]], [[4ijl]], [[4iph]], [[4luo]], [[4luv]], [[4luz]], [[4lw1]], [[4lwc]], [[4o0a]] – hSSB N terminal domain (mutant) + inhibitor<br />
 
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===Replication protein A===
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''RPA70''
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[[1ewi]], [[2b29]] - hRPA70 N terminal - NMR<br />
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[[4ipc]], [[4ipd]], [[4ipg]] - hRPA70 N terminal (mutant) <br />
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[[1fgu]] – hRPA70 central domain <br />
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[[1ynx]] – yRPA69 DBD-A – yeast – NMR<br />
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[[1jmc]] – hRPA70 central domain + DNA <br />
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[[2b3g]] - hRPA70 N terminal + p53 peptide<br />
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[[4nb3]] - hRPA70 N terminal (mutant) + peptide<br />
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[[4ijh]], [[4ijl]], [[4iph]], [[4luo]], [[4luv]], [[4luz]], [[4lw1]], [[4lwc]], [[4o0a]] - hRPA70 N terminal (mutant) + inhibitor<br />
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''RPA14 + RPA32 + RPA70''
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[[1l1o]] – hRPA14 + hRPA32 central domain + hRPA70 C terminal <br />
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 08:59, 27 July 2014

Image:1eqq.png
Crystal structure of SSB complex with ssDNA 1eqq

Template:STRUCTURE 1eqq












Single-stranded DNA-binding protein (SSB) binds to single-stranded regions of DNA (ssDNA) to protect it from annealing, prevention of secondary structure formation and digestion. SSB binds to DNA in a sequence-independent manner. The binding of SSB enables processes like replication, DNA repair and recombination to occur. SSB can form complexes with specific genome maintenance proteins helping their activities. Viral SSB proteins are monomeric while eukaryotic SSB (Replication protein A – RPA) is a heterotrimer composed of RPA70, RPA32 and RPA14. RPA has 6 DNA-binding domains (DBD). The mitochondrial human SSB (HsmtSSB) is a homotetramer. See also Single stranded binding protein.

Contents

3D Structures of single-stranded DNA-binding protein

Updated on 27-July-2014

1gpc – SSB gp32 – Enterobacteria phage T4
2a1k – SSB gp32 – Enterobacteria phage RB69
1je5 – SSB – Enterobacteria phage T7
1adu, 1adv, 1anv – SSB C terminal – human adenovirus 5
1urj – SSB – human herpesvirus 1
1pfs – SSB (mutant) – Pseudomonas phage PF3 - NMR
3ull, 1s3o, 2dud – HsmtSSB residues 16-148 – human
1kaw – EcSSB chymotryptic domain – Escherichia coli
1qvc, 1sru – EcSSB
1o7i – SSB residues 1-119 – Sulfolobus solfataricus
1ue1, 1ue5, 1ue7, 1ue6 – SSB – Mycobacterium tuberculosis
1x3e, 1x3f, 1x3g – MsSSB – Mycobacterium smegmatis
1se8 – DrSSB – Deinococcus radiodurans
4exw – SSB DdrB – Deinococcus geothermalis
1z9f – SSB – Thermotoga maritima
2cwa – SSB – Thermus thermophilus
2fxq, 2ihe – TaSSB – Thermus aquaticus
2ihf – TaSSB (mutant)
2hql – SSB – Mycoplasma pneumoniae
3eiv – ScSSB – Streptomyces coelicolor
4dam – ScSSB (mutant)
3lgj, 3pgz – SSB – Bartonella henselae
3afp, 3afq – SSB – Mycobacterium leprae
3tqy – SSB – Coxiella burnetii
3tek – SSB N terminal – Thermoproteus tenax
4gs3 – SSB N terminal – Thermoanaerobacter tengcongensis
3dm3 – SSB A domain – Methancaldococcus jannaschii
1vqe, 1yha, 1vqb – F1SSB – Enterobacteria phage F1
2gn5 – M13SSB – Enterobacteria phage M13
2gva, 2gvb – M13SSB (mutant) - NMR
1vqa, 1vqc, 1vqd, 1vqe, 1vqf, 1vqg, 1vqh, 1vqi, 1vqj, 1ae2, 1ae3, 1gkh, 1SSB – F1SSB (mutant)

SSB complex with ssDNA

1eyg – EcSSB chymotryptic domain + ssDNA
1eqq – EcSSB + ssDNA
2vw9 – HpSSB + ssDNA
3vdy – SSB + ssDNA – Bacillus subtilis
3a5u – MsSSB chymotryptic domain + ssDNA
3udg – DrSSB + ssDNA

SSB other complexes

3ufm, 3uf7 – DrSSB C terminal + uracil-DNA glycosylase

Replication protein A

RPA70

1ewi, 2b29 - hRPA70 N terminal - NMR
4ipc, 4ipd, 4ipg - hRPA70 N terminal (mutant)
1fgu – hRPA70 central domain
1ynx – yRPA69 DBD-A – yeast – NMR
1jmc – hRPA70 central domain + DNA
2b3g - hRPA70 N terminal + p53 peptide
4nb3 - hRPA70 N terminal (mutant) + peptide
4ijh, 4ijl, 4iph, 4luo, 4luv, 4luz, 4lw1, 4lwc, 4o0a - hRPA70 N terminal (mutant) + inhibitor

RPA14 + RPA32 + RPA70

1l1o – hRPA14 + hRPA32 central domain + hRPA70 C terminal

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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