1je5

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==Crystal Structure of gp2.5, a Single-Stranded DNA Binding Protein Encoded by Bacteriophage T7==
==Crystal Structure of gp2.5, a Single-Stranded DNA Binding Protein Encoded by Bacteriophage T7==
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<StructureSection load='1je5' size='340' side='right' caption='[[1je5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='1je5' size='340' side='right'caption='[[1je5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1je5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt7 Bpt7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JE5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JE5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1je5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T7 Escherichia phage T7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JE5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JE5 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1je5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1je5 OCA], [http://pdbe.org/1je5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1je5 RCSB], [http://www.ebi.ac.uk/pdbsum/1je5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1je5 ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1je5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1je5 OCA], [https://pdbe.org/1je5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1je5 RCSB], [https://www.ebi.ac.uk/pdbsum/1je5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1je5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DNBI_BPT7 DNBI_BPT7]] Single-stranded DNA-binding protein that eliminates secondary structure in long ssDNA formed on the lagging strand of the replication fork. Stimulates DNA polymerase activity and increases the efficiency of RNA primer synthesis by interacting with the DNA polymerase and the helicase/primase protein gp4. Disrupts loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation.<ref>PMID:1634538</ref> <ref>PMID:16807232</ref> <ref>PMID:8106511</ref>
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[https://www.uniprot.org/uniprot/SSB_BPT7 SSB_BPT7] Single-stranded DNA-binding protein that participates in viral DNA replication, formation of concatemers, recombination and repair of double-stranded breaks (PubMed:16807232, PubMed:8617248, PubMed:9079662, PubMed:11222583). Coats the lagging-strand ssDNA as the replication fork advances and stimulates the activities of viral DNA polymerase and primase/helicase (PubMed:8617248). Coordinates simultaneous synthesis of leading- and lagging-strands (PubMed:9651583). Together with DNA primase/helicase, promotes pairing of two homologous DNA molecules containing complementary single-stranded regions and mediates homologous DNA strand exchange (PubMed:8617248). Promotes also the formation of joint molecules (PubMed:8617248, PubMed:9079662). Disrupts loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation (PubMed:1634538).[HAMAP-Rule:MF_04153]<ref>PMID:11222583</ref> <ref>PMID:1634538</ref> <ref>PMID:16807232</ref> <ref>PMID:8617248</ref> <ref>PMID:9079662</ref> <ref>PMID:9651583</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1je5 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1je5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The gene 2.5 protein (gp2.5) of bacteriophage T7 is a single-stranded DNA (ssDNA) binding protein that has essential roles in DNA replication and recombination. In addition to binding DNA, gp2.5 physically interacts with T7 DNA polymerase and T7 primase-helicase during replication to coordinate events at the replication fork. We have determined a 1.9-A crystal structure of gp2.5 and show that it has a conserved OB-fold (oligosaccharide/oligonucleotide binding fold) that is well adapted for interactions with ssDNA. Superposition of the OB-folds of gp2.5 and other ssDNA binding proteins reveals a conserved patch of aromatic residues that stack against the bases of ssDNA in the other crystal structures, suggesting that gp2.5 binds to ssDNA in a similar manner. An acidic C-terminal extension of the gp2.5 protein, which is required for dimer formation and for interactions with the T7 DNA polymerase and the primase-helicase, appears to be flexible and may act as a switch that modulates the DNA binding affinity of gp2.5.
 
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Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7.,Hollis T, Stattel JM, Walther DS, Richardson CC, Ellenberger T Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9557-62. Epub 2001 Jul 31. PMID:11481454<ref>PMID:11481454</ref>
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==See Also==
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*[[Single-stranded DNA-binding protein 3D structures|Single-stranded DNA-binding protein 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1je5" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bpt7]]
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[[Category: Escherichia phage T7]]
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[[Category: Ellenberger, T E]]
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[[Category: Large Structures]]
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[[Category: Hollis, T]]
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[[Category: Ellenberger TE]]
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[[Category: Richardson, C C]]
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[[Category: Hollis T]]
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[[Category: Stattel, J M]]
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[[Category: Richardson CC]]
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[[Category: Walther, D S]]
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[[Category: Stattel JM]]
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[[Category: Beta barrel]]
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[[Category: Walther DS]]
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[[Category: Dna binding protein]]
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[[Category: Ob-fold]]
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Current revision

Crystal Structure of gp2.5, a Single-Stranded DNA Binding Protein Encoded by Bacteriophage T7

PDB ID 1je5

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