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1taq

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[[Image:1taq.gif|left|200px]]
 
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{{Structure
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==STRUCTURE OF TAQ DNA POLYMERASE==
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|PDB= 1taq |SIZE=350|CAPTION= <scene name='initialview01'>1taq</scene>, resolution 2.4&Aring;
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<StructureSection load='1taq' size='340' side='right'caption='[[1taq]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1taq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TAQ FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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]] 2.4&#8491;</td></tr>
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|GENE= TAQ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=271 Thermus aquaticus])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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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=1taq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1taq OCA], [https://pdbe.org/1taq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1taq RCSB], [https://www.ebi.ac.uk/pdbsum/1taq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1taq ProSAT]</span></td></tr>
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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1taq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1taq OCA], [http://www.ebi.ac.uk/pdbsum/1taq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1taq RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DPO1_THEAQ DPO1_THEAQ]
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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/ta/1taq_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=1taq ConSurf].
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<div style="clear:both"></div>
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'''STRUCTURE OF TAQ DNA POLYMERASE'''
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==See Also==
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*[[DNA polymerase|DNA polymerase]]
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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==Overview==
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__TOC__
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The DNA polymerase from Thermus aquaticus (Taq polymerase), famous for its use in the polymerase chain reaction, is homologous to Escherichia coli DNA polymerase I (pol I) Like pol I, Taq polymerase has a domain at its amino terminus (residues 1-290) that has 5' nuclease activity and a domain at its carboxy terminus that catalyses the polymerase reaction. Unlike pol I, the intervening domain in Taq polymerase has lost the editing 3'-5' exonuclease activity. Although the structure of the Klenow fragment of pol I has been known for ten years, that of the intact pol I has proved more elusive. The structure of Taq polymerase determined here at 2.4 A resolution shows that the structures of the polymerase domains of the thermostable enzyme and of the Klenow fragment are nearly identical, whereas the catalytically critical carboxylate residues that bind two metal ions are missing from the remnants of the 3'-5' exonuclease active site of Taq polymerase. The first view of the 5' nuclease domain, responsible for excising the Okazaki RNA in lagging-strand DNA replication, shows a cluster of conserved divalent metal-ion-binding carboxylates at the bottom of a cleft. The location of this 5'-nuclease active site some 70 A from the polymerase active site in this crystal form highlights the unanswered question of how this domain works in concert with the polymerase domain to produce a duplex DNA product that contains only a nick.
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</StructureSection>
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[[Category: Large Structures]]
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==About this Structure==
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1TAQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAQ OCA].
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==Reference==
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Crystal structure of Thermus aquaticus DNA polymerase., Kim Y, Eom SH, Wang J, Lee DS, Suh SW, Steitz TA, Nature. 1995 Aug 17;376(6541):612-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7637814 7637814]
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[[Category: DNA-directed DNA polymerase]]
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[[Category: Single protein]]
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[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
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[[Category: Eom, S H.]]
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[[Category: Eom SH]]
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[[Category: Kim, Y.]]
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[[Category: Kim Y]]
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[[Category: Lee, D S.]]
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[[Category: Lee D-S]]
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[[Category: Steitz, T A.]]
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[[Category: Steitz TA]]
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[[Category: Suh, S W.]]
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[[Category: Suh SW]]
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[[Category: Wang, J.]]
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[[Category: Wang J]]
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[[Category: nucleotidyltransferase]]
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[[Category: pcr polymerase]]
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[[Category: taq dna polymerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:53:38 2008''
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Current revision

STRUCTURE OF TAQ DNA POLYMERASE

PDB ID 1taq

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