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New page: left|200px<br /><applet load="2hpm" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hpm, resolution 3.70Å" /> '''Eubacterial and Euka...
 
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[[Image:2hpm.gif|left|200px]]<br /><applet load="2hpm" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2hpm, resolution 3.70&Aring;" />
'''Eubacterial and Eukaryotic Replicative DNA Polymerases are not Homologous: X-ray Structure of DNA Polymerase III'''<br />


==Overview==
==Eubacterial and Eukaryotic Replicative DNA Polymerases are not Homologous: X-ray Structure of DNA Polymerase III==
The crystal structure of Thermus aquaticus DNA polymerase III alpha, subunit reveals that the structure of the catalytic domain of the, eubacterial replicative polymerase is unrelated to that of the eukaryotic, replicative polymerase but rather belongs to the Polbeta-like, nucleotidyltransferase superfamily. A model of the polymerase complexed, with both DNA and beta-sliding clamp interacting with a reoriented binding, domain and internal beta binding site was constructed that is consistent, with existing biochemical data. Within the crystal, two C-terminal domains, are interacting through a surface that is larger than many dimer, interfaces. Since replicative polymerases of eubacteria and, eukaryotes/archaea are not homologous, the nature of the replicative, polymerase in the last common ancestor is unknown. Although other, possibilities have been proposed, the plausibility of a ribozyme DNA, polymerase should be considered.
<StructureSection load='2hpm' size='340' side='right'caption='[[2hpm]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2hpm]] 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=2HPM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HPM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PO:TRIPHOSPHATE'>3PO</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2hpm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hpm OCA], [https://pdbe.org/2hpm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hpm RCSB], [https://www.ebi.ac.uk/pdbsum/2hpm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hpm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DPO3A_THEAQ DPO3A_THEAQ] DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hp/2hpm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2hpm ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2HPM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with ZN, MG, CL and 3PO as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2HPM OCA].
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The structure of T. aquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases., Bailey S, Wing RA, Steitz TA, Cell. 2006 Sep 8;126(5):893-904. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16959569 16959569]
[[Category: Large Structures]]
[[Category: DNA-directed DNA polymerase]]
[[Category: Single protein]]
[[Category: Thermus aquaticus]]
[[Category: Thermus aquaticus]]
[[Category: Bailey, S.]]
[[Category: Bailey S]]
[[Category: Steitz, T.A.]]
[[Category: Steitz TA]]
[[Category: Wing, R.A.]]
[[Category: Wing RA]]
[[Category: 3PO]]
[[Category: CL]]
[[Category: MG]]
[[Category: ZN]]
[[Category: nucleotidyltransferase fold]]
 
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Retrieved from "https://proteopedia.org/2hpm"