1ktq
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ktq' size='340' side='right'caption='[[1ktq]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1ktq' size='340' side='right'caption='[[1ktq]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1ktq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1ktq]] 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=1KTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KTQ FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> |
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ktq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ktq OCA], [https://pdbe.org/1ktq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ktq RCSB], [https://www.ebi.ac.uk/pdbsum/1ktq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ktq ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ktq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ktq OCA], [https://pdbe.org/1ktq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ktq RCSB], [https://www.ebi.ac.uk/pdbsum/1ktq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ktq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/DPO1_THEAQ DPO1_THEAQ] | ||
== 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=1ktq 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=1ktq ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The crystal structure of the large fragment of the Thermus aquaticus DNA polymerase (Klentaq1), determined at 2.5-A resolution, demonstrates a compact two-domain architecture. The C-terminal domain is identical in fold to the equivalent region of the Klenow fragment of Escherichia coli DNA polymerase I (Klenow pol I). Although the N-terminal domain of Klentaq1 differs greatly in sequence from its counterpart in Klenow pol I, it has clearly evolved from a common ancestor. The structure of Klentaq1 reveals the strategy utilized by this protein to maintain activity at high temperatures and provides the structural basis for future improvements of the enzyme. | ||
- | + | ==See Also== | |
- | + | *[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | |
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: Atcc 25104]] | ||
- | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Thermus aquaticus]] |
- | [[Category: | + | [[Category: Korolev S]] |
- | [[Category: | + | [[Category: Waksman G]] |
- | + |
Current revision
DNA POLYMERASE
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