5omc: Difference between revisions

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<StructureSection load='5omc' size='340' side='right'caption='[[5omc]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
<StructureSection load='5omc' size='340' side='right'caption='[[5omc]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5omc]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OMC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OMC FirstGlance]. <br>
<table><tr><td colspan='2'>[[5omc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Kluyveromyces_lactis Kluyveromyces lactis] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5OMC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.38&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5omc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5omc OCA], [http://pdbe.org/5omc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5omc RCSB], [http://www.ebi.ac.uk/pdbsum/5omc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5omc ProSAT]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=5omc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5omc OCA], [https://pdbe.org/5omc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5omc RCSB], [https://www.ebi.ac.uk/pdbsum/5omc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5omc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/RFA1_YEAST RFA1_YEAST]] Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication. [[http://www.uniprot.org/uniprot/LCD1_KLULA LCD1_KLULA]] Forms a complex with the serine/threonine kinase MEC1 which activates checkpoint signaling upon genotoxic stresses. The MEC1-LCD1 complex is recruited to DNA lesions in order to initiates the DNA repair by homologous recombination. Required for cell growth and meiotic recombination (By similarity).  
[https://www.uniprot.org/uniprot/RFA1_YEAST RFA1_YEAST] Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Kluyveromyces lactis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Deshpande, I]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Gasser, S M]]
[[Category: Deshpande I]]
[[Category: Gut, H]]
[[Category: Gasser SM]]
[[Category: Keusch, J J]]
[[Category: Gut H]]
[[Category: Seeber, A]]
[[Category: Keusch JJ]]
[[Category: Shimada, K]]
[[Category: Seeber A]]
[[Category: Coiled-coil domain]]
[[Category: Shimada K]]
[[Category: Complex]]
[[Category: Mutant]]
[[Category: Oligonucleotide-binding fold]]
[[Category: Protein binding]]