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1tgo

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(New page: 200px<br /><applet load="1tgo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tgo, resolution 2.5&Aring;" /> '''THERMOSTABLE B TYPE D...)
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[[Image:1tgo.jpg|left|200px]]<br /><applet load="1tgo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1tgo, resolution 2.5&Aring;" />
 
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'''THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS'''<br />
 
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==Overview==
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==THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS==
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Most known archaeal DNA polymerases belong to the type B family, which, also includes the DNA replication polymerases of eukaryotes, but maintain, high fidelity at extreme conditions. We describe here the 2.5 A resolution, crystal structure of a DNA polymerase from the Archaea Thermococcus, gorgonarius and identify structural features of the fold and the active, site that are likely responsible for its thermostable function. Comparison, with the mesophilic B type DNA polymerase gp43 of the bacteriophage RB69, highlights thermophilic adaptations, which include the presence of two, disulfide bonds and an enhanced electrostatic complementarity at the, DNA-protein interface. In contrast to gp43, several loops in the, exonuclease and thumb domains are more closely packed; this apparently, blocks primer binding to the exonuclease active site. A physiological role, of this "closed" conformation is unknown but may represent a polymerase, mode, in contrast to an editing mode with an open exonuclease site. This, archaeal B DNA polymerase structure provides a starting point for, structure-based design of polymerases or ligands with applications in, biotechnology and the development of antiviral or anticancer agents.
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<StructureSection load='1tgo' size='340' side='right'caption='[[1tgo]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1tgo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermococcus_gorgonarius Thermococcus gorgonarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TGO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TGO FirstGlance]. <br>
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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]] 2.5&#8491;</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=1tgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tgo OCA], [https://pdbe.org/1tgo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tgo RCSB], [https://www.ebi.ac.uk/pdbsum/1tgo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tgo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/DPOL_THEGO DPOL_THEGO] In addition to polymerase activity, this DNA polymerase exhibits 3' to 5' exonuclease activity.
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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/tg/1tgo_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=1tgo ConSurf].
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<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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Most known archaeal DNA polymerases belong to the type B family, which also includes the DNA replication polymerases of eukaryotes, but maintain high fidelity at extreme conditions. We describe here the 2.5 A resolution crystal structure of a DNA polymerase from the Archaea Thermococcus gorgonarius and identify structural features of the fold and the active site that are likely responsible for its thermostable function. Comparison with the mesophilic B type DNA polymerase gp43 of the bacteriophage RB69 highlights thermophilic adaptations, which include the presence of two disulfide bonds and an enhanced electrostatic complementarity at the DNA-protein interface. In contrast to gp43, several loops in the exonuclease and thumb domains are more closely packed; this apparently blocks primer binding to the exonuclease active site. A physiological role of this "closed" conformation is unknown but may represent a polymerase mode, in contrast to an editing mode with an open exonuclease site. This archaeal B DNA polymerase structure provides a starting point for structure-based design of polymerases or ligands with applications in biotechnology and the development of antiviral or anticancer agents.
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==About this Structure==
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Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius.,Hopfner KP, Eichinger A, Engh RA, Laue F, Ankenbauer W, Huber R, Angerer B Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3600-5. PMID:10097083<ref>PMID:10097083</ref>
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1TGO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermococcus_gorgonarius Thermococcus gorgonarius]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TGO OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius., Hopfner KP, Eichinger A, Engh RA, Laue F, Ankenbauer W, Huber R, Angerer B, Proc Natl Acad Sci U S A. 1999 Mar 30;96(7):3600-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10097083 10097083]
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</div>
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[[Category: DNA-directed DNA polymerase]]
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<div class="pdbe-citations 1tgo" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Thermococcus gorgonarius]]
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[[Category: Angerer, B.]]
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[[Category: Ankenbauer, W.]]
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[[Category: Eichinger, A.]]
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[[Category: Engh, R.A.]]
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[[Category: Hopfner, K.P.]]
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[[Category: Huber, R.]]
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[[Category: Laue, F.]]
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[[Category: disulfide bonds]]
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[[Category: dna polymerase]]
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[[Category: replication]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:15:00 2007''
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==See Also==
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*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Thermococcus gorgonarius]]
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[[Category: Angerer B]]
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[[Category: Ankenbauer W]]
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[[Category: Eichinger A]]
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[[Category: Engh RA]]
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[[Category: Hopfner K-P]]
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[[Category: Huber R]]
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[[Category: Laue F]]

Current revision

THERMOSTABLE B TYPE DNA POLYMERASE FROM THERMOCOCCUS GORGONARIUS

PDB ID 1tgo

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