2hix: Difference between revisions

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 <StructureSection load='2hix' size='340' side='right'caption='[[2hix]], [[Resolution|resolution]] 2.87&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2hix]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HIX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2hix]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HIX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.87&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hii|2hii]], [[2hik|2hik]], [[2hiv|2hiv]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lig ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/DNA_ligase_(ATP) DNA ligase (ATP)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.5.1.1 6.5.1.1] </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=2hix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hix OCA], [https://pdbe.org/2hix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hix RCSB], [https://www.ebi.ac.uk/pdbsum/2hix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hix ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/DNLI_SULSO DNLI_SULSO]] DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Interaction with PCNA enhances ligase activity.[HAMAP-Rule:MF_00407]
+[https://www.uniprot.org/uniprot/DNLI_SACS2 DNLI_SACS2] DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Interaction with PCNA enhances ligase activity. DNA polymerase I, DNA ligase and the flap endonuclease may be constitutively associated with the PCNA heterotrimer forming a scanning complex able to couple DNA synthesis and Okazaki fragment maturation.<ref>PMID:12535540</ref>
 == Evolutionary Conservation ==
 [[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=2hix ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-DNA sliding clamps encircle DNA and provide binding sites for many DNA-processing enzymes. However, it is largely unknown how sliding clamps like proliferating cell nuclear antigen (PCNA) coordinate multistep DNA transactions. We have determined structures of Sulfolobus solfataricus DNA ligase and heterotrimeric PCNA separately by X-ray diffraction and in complex by small-angle X-ray scattering (SAXS). Three distinct PCNA subunits assemble into a protein ring resembling the homotrimeric PCNA of humans but with three unique protein-binding sites. In the absence of nicked DNA, the Sulfolobus solfataricus DNA ligase has an open, extended conformation. When complexed with heterotrimeric PCNA, the DNA ligase binds to the PCNA3 subunit and ligase retains an open, extended conformation. A closed, ring-shaped conformation of ligase catalyzes a DNA end-joining reaction that is strongly stimulated by PCNA. This open-to-closed switch in the conformation of DNA ligase is accommodated by a malleable interface with PCNA that serves as an efficient platform for DNA ligation.
-A flexible interface between DNA ligase and PCNA supports conformational switching and efficient ligation of DNA.,Pascal JM, Tsodikov OV, Hura GL, Song W, Cotner EA, Classen S, Tomkinson AE, Tainer JA, Ellenberger T Mol Cell. 2006 Oct 20;24(2):279-91. PMID:17052461<ref>PMID:17052461</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2hix" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 39: / Line 28: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 35091]]
 [[Category: Large Structures]]
-[[Category: Ellenberger, T]]
+[[Category: Saccharolobus solfataricus]]
-[[Category: Pascal, J M]]
+[[Category: Ellenberger T]]
-[[Category: Atp-dependent dna ligase]]
+[[Category: Pascal JM]]
-[[Category: Dna replication]]
-[[Category: Ligase]]