1du2: Difference between revisions

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-{{Seed}}
-[[Image:1du2.png|left|200px]]
-<!--
+==SOLUTION STRUCTURE OF THE THETA SUBUNIT OF DNA POLYMERASE III==
-The line below this paragraph, containing "STRUCTURE_1du2", creates the "Structure Box" on the page.
+<StructureSection load='1du2' size='340' side='right'caption='[[1du2]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1du2]] 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=1DU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DU2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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=1du2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1du2 OCA], [https://pdbe.org/1du2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1du2 RCSB], [https://www.ebi.ac.uk/pdbsum/1du2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1du2 ProSAT]</span></td></tr>
-{{STRUCTURE_1du2|  PDB=1du2  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HOLE_ECOLI HOLE_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.  The exact function of the theta subunit is unknown.
+== 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/du/1du2_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=1du2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The catalytic core of Escherichia coli DNA polymerase III contains three tightly associated subunits (alpha, epsilon, and theta). The theta subunit is the smallest, but the least understood of the three. As a first step in a program aimed at understanding its function, the structure of the theta subunit has been determined by triple-resonance multidimensional NMR spectroscopy. Although only a small protein, theta was difficult to assign fully because approximately one-third of the protein is unstructured, and some sections of the remaining structured parts undergo intermediate intramolecular exchange. The secondary structure was deduced from the characteristic nuclear Overhauser effect patterns, the 3J(HN alpha) coupling constants and the consensus chemical shift index. The C-terminal third of the protein, which has many charged and hydrophilic amino acid residues, has no well-defined secondary structure and exists in a highly dynamic state. The N-terminal two-thirds has three helical segments (Gln10-Asp19, Glu38-Glu43, and His47-Glu54), one short extended segment (Pro34-Ala37), and a long loop (Ala20-Glu29), of which part may undergo intermediate conformational exchange. Solution of the three-dimensional structure by NMR techniques revealed that the helices fold in such a way that the surface of theta is bipolar, with one face of the protein containing most of the acidic residues and the other face containing most of the long chain basic residues. Preliminary chemical shift mapping experiments with a domain of the epsilon subunit have identified a loop region (Ala20-Glu29) in theta as the site of association with epsilon.
-===SOLUTION STRUCTURE OF THE THETA SUBUNIT OF DNA POLYMERASE III===
+NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli.,Keniry MA, Berthon HA, Yang JY, Miles CS, Dixon NE Protein Sci. 2000 Apr;9(4):721-33. PMID:10794414<ref>PMID:10794414</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1du2" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10794414}}, adds the Publication Abstract to the page
+*[[DNA polymerase 3D structures|DNA polymerase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10794414 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10794414}}
+__TOC__
+</StructureSection>
-==About this Structure==
-DU2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DU2 OCA].
-==Reference==
-NMR solution structure of the theta subunit of DNA polymerase III from Escherichia coli., Keniry MA, Berthon HA, Yang JY, Miles CS, Dixon NE, Protein Sci. 2000 Apr;9(4):721-33. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10794414 10794414]
-[[Category: DNA-directed DNA polymerase]]
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Berthon, H A.]]
+[[Category: Berthon HA]]
-[[Category: Dixon, N E.]]
+[[Category: Dixon NE]]
-[[Category: Keniry, M A.]]
+[[Category: Keniry MA]]
-[[Category: Miles, C S.]]
+[[Category: Miles CS]]
-[[Category: Yang, J Y.]]
+[[Category: Yang J-Y]]
-[[Category: Alpha helix]]
-[[Category: Dna polymerase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:37:03 2008''