1t7p

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[[Image:1t7p.gif|left|200px]]
 
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{{Structure
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==T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN==
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|PDB= 1t7p |SIZE=350|CAPTION= <scene name='initialview01'>1t7p</scene>, resolution 2.2&Aring;
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<StructureSection load='1t7p' size='340' side='right'caption='[[1t7p]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=DG3:2&#39;-3&#39;-DIDEOXYGUANOSINE-5&#39;-TRIPHOSPHATE'>DG3</scene>
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<table><tr><td colspan='2'>[[1t7p]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7] and [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=1T7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T7P FirstGlance]. <br>
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|ACTIVITY= [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7]
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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]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2DA:2,3-DIDEOXYADENOSINE-5-MONOPHOSPHATE'>2DA</scene>, <scene name='pdbligand=DG3:2-3-DIDEOXYGUANOSINE-5-TRIPHOSPHATE'>DG3</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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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=1t7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t7p OCA], [https://pdbe.org/1t7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t7p RCSB], [https://www.ebi.ac.uk/pdbsum/1t7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t7p ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t7/1t7p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1t7p ConSurf].
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<div style="clear:both"></div>
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'''T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN'''
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==See Also==
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
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==Overview==
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== References ==
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DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10(-5) to 10(-6). Here we present a 2.2 A crystal structure of the replicative DNA polymerase from bacteriophage T7 complexed with a primer-template and a nucleoside triphosphate in the polymerase active site. The structure illustrates how nucleotides are selected in a template-directed manner, and provides a structural basis for a metal-assisted mechanism of phosphoryl transfer by a large group of related polymerases.
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<references/>
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__TOC__
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==About this Structure==
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</StructureSection>
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1T7P is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7P OCA].
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[[Category: Escherichia coli O157:H7]]
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[[Category: Escherichia phage T7]]
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==Reference==
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[[Category: Large Structures]]
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Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution., Doublie S, Tabor S, Long AM, Richardson CC, Ellenberger T, Nature. 1998 Jan 15;391(6664):251-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9440688 9440688]
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[[Category: Doublie S]]
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[[Category: Bacteriophage t7]]
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[[Category: Ellenberger T]]
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[[Category: DNA-directed DNA polymerase]]
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[[Category: Long AM]]
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[[Category: Escherichia coli]]
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[[Category: Richardson CC]]
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[[Category: Protein complex]]
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[[Category: Tabor S]]
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[[Category: Doublie, S.]]
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[[Category: Ellenberger, T.]]
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[[Category: Long, A M.]]
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[[Category: Richardson, C C.]]
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[[Category: Tabor, S.]]
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[[Category: DG3]]
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[[Category: MG]]
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[[Category: complex (hydrolase/electron transport/dna)]]
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[[Category: dna replication]]
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[[Category: nucleotidyl transferase]]
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[[Category: processivity factor]]
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[[Category: sequencing]]
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[[Category: t7 dna polymerase]]
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[[Category: thioredoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 13:42:15 2008''
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Current revision

T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN

PDB ID 1t7p

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