1vpk: Difference between revisions
New page: left|200px<br /><applet load="1vpk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vpk, resolution 2.00Å" /> '''Crystal structure of... |
No edit summary |
||
(17 intermediate revisions by the same user not shown) | |||
Line 1: | Line 1: | ||
== | ==Crystal structure of DNA polymerase III, beta subunit (TM0262) from Thermotoga maritima at 2.00 A resolution== | ||
<StructureSection load='1vpk' size='340' side='right'caption='[[1vpk]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
[[ | == Structural highlights == | ||
[ | <table><tr><td colspan='2'>[[1vpk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VPK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VPK 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]] 2Å</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=1vpk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vpk OCA], [https://pdbe.org/1vpk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vpk RCSB], [https://www.ebi.ac.uk/pdbsum/1vpk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vpk ProSAT], [https://www.topsan.org/Proteins/JCSG/1vpk TOPSAN]</span></td></tr> | ||
</table> | |||
[[ | == Function == | ||
[https://www.uniprot.org/uniprot/Q9WYA0_THEMA Q9WYA0_THEMA] 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 beta chain is required for initiation of replication once it is clamped onto DNA, it slides freely (bidirectional and ATP-independent) along duplex DNA (By similarity).[PIRNR:PIRNR000804] | |||
== 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/vp/1vpk_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=1vpk ConSurf]. | |||
<div style="clear:both"></div> | |||
==See Also== | |||
*[[DNA polymerase 3D structures|DNA polymerase 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermotoga maritima MSB8]] |