View source for 2aya


==Solution Structure of the C-Terminal 14 kDa Domain of the tau subunit from Escherichia coli DNA Polymerase III==
<StructureSection load='2aya' size='340' side='right'caption='[[2aya]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2aya]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AYA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2aya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aya OCA], [https://pdbe.org/2aya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aya RCSB], [https://www.ebi.ac.uk/pdbsum/2aya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aya ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DPO3X_ECOLI DPO3X_ECOLI] 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.  Isoform tau: serves as a scaffold to help in the dimerization of the core complex.  Isoform gamma: seems to interact with the delta subunit. to transfer the beta subunit on the DNA.
== 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/ay/2aya_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=2aya ConSurf].
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== Publication Abstract from PubMed ==
The solution structure of the C-terminal Domain V of the tau subunit of E. coli DNA polymerase III was determined by nuclear magnetic resonance (NMR) spectroscopy. The fold is unique to tau subunits. Amino acid sequence conservation is pronounced for hydrophobic residues that form the structural core of the protein, indicating that the fold is representative for tau subunits from a wide range of different bacteria. The interaction between the polymerase subunits tau and alpha was studied by NMR experiments where alpha was incubated with full-length C-terminal domain (tau(C)16), and domains shortened at the C-terminus by 11 and 18 residues, respectively. The only interacting residues were found in the C-terminal 30-residue segment of tau, most of which is structurally disordered in free tau(C)16. Since the N- and C-termini of the structured core of tau(C)16 are located close to each other, this limits the possible distance between alpha and the pentameric deltatau2gammadelta' clamp-loader complex and, hence, between the two alpha subunits involved in leading- and lagging-strand DNA synthesis. Analysis of an N-terminally extended construct (tau(C)22) showed that tau(C)14 presents the only part of Domains IVa and V of tau which comprises a globular fold in the absence of other interaction partners.

Solution structure of Domains IVa and V of the tau subunit of Escherichia coli DNA polymerase III and interaction with the alpha subunit.,Su XC, Jergic S, Keniry MA, Dixon NE, Otting G Nucleic Acids Res. 2007;35(9):2825-32. Epub 2007 Apr 22. PMID:17452361<ref>PMID:17452361</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2aya" style="background-color:#fffaf0;"></div>

==See Also==
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Dixon NE]]
[[Category: Jergic S]]
[[Category: Otting G]]
[[Category: Su XC]]