5ikn

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'''Unreleased structure'''
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{{Large structure}}
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==Crystal Structure of the T7 Replisome in the Absence of DNA==
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The entry 5ikn is ON HOLD until Paper Publication
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<StructureSection load='5ikn' size='340' side='right' caption='[[5ikn]], [[Resolution|resolution]] 4.80&Aring;' scene=''>
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== Structural highlights ==
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Authors: Wallen, J.R., Ellenberger, T.
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<table><tr><td colspan='2'>[[5ikn]] is a 13 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5IKN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IKN FirstGlance]. <br>
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</td></tr><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=5ikn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ikn OCA], [http://pdbe.org/5ikn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ikn RCSB], [http://www.ebi.ac.uk/pdbsum/5ikn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ikn ProSAT]</span></td></tr>
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Description: Crystal Structure of the T7 Replisome in the Absence of DNA
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</table>
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[[Category: Unreleased Structures]]
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{{Large structure}}
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== Function ==
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[[http://www.uniprot.org/uniprot/DPOL_BPT7 DPOL_BPT7]] Replicates viral genomic DNA. Non-processive DNA polymerase that achieves processivity by binding to host thioredoxin (TrxA). This interaction increases the rate of dNTP incorporation to yield a processivity of approximately 800 nucleotides (nt) per binding event. Interacts with DNA helicase gp4 to coordinate nucleotide polymerization with unwinding of the DNA. The leading strand is synthesized continuously while synthesis of the lagging strand requires the synthesis of oligoribonucleotides by the primase domain of gp4.<ref>PMID:9218486</ref> <ref>PMID:21606333</ref> [[http://www.uniprot.org/uniprot/THIO_ECO57 THIO_ECO57]] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions (By similarity). [[http://www.uniprot.org/uniprot/PRIM_BPT7 PRIM_BPT7]] Synthesizes short RNA primers for DNA replication. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase elongates using dNTPs.<ref>PMID:9096333</ref> <ref>PMID:21606333</ref> <ref>PMID:22977246</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Ellenberger, T]]
[[Category: Ellenberger, T]]
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[[Category: Wallen, J.R]]
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[[Category: Wallen, J R]]
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[[Category: Replisome]]
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[[Category: Transferase]]

Revision as of 02:14, 11 December 2016

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Crystal Structure of the T7 Replisome in the Absence of DNA

5ikn, resolution 4.80Å

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