4xlg: Difference between revisions
New page: '''Unreleased structure''' The entry 4xlg is ON HOLD Authors: Gaur, V., Wyatt, H.D.M., Komorowska, W., Szczepanowski, R.H., de Sanctis, D., Gorecka, K.M., West, S.C., Nowotny, M. Descr... |
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The | ==C. glabrata Slx1 in complex with Slx4CCD.== | ||
<StructureSection load='4xlg' size='340' side='right'caption='[[4xlg]], [[Resolution|resolution]] 1.78Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4xlg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_glabrata_CBS_138 Candida glabrata CBS 138]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XLG 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]] 1.78Å</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>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4xlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xlg OCA], [https://pdbe.org/4xlg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xlg RCSB], [https://www.ebi.ac.uk/pdbsum/4xlg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xlg ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SLX4_CANGA SLX4_CANGA] Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The SLX1-SLX4 endonuclease required for homologous recombination and DNA repair in eukaryotic cells cleaves a variety of branched DNA structures. The nuclease subunit SLX1 is activated by association with a scaffolding protein SLX4. At the present time, little is known about the structure of SLX1-SLX4 or its mechanism of action. Here, we report the structural insights into SLX1-SLX4 by detailing the crystal structure of Candida glabrata (Cg) Slx1 alone and in combination with the C-terminal region of Slx4. The structure of Slx1 reveals a compact arrangement of the GIY-YIG nuclease and RING domains, which is reinforced by a long alpha helix. Slx1 forms a stable homodimer that blocks its active site. Slx1-Slx4 interaction is mutually exclusive with Slx1 homodimerization, suggesting a mechanism for Slx1 activation by Slx4. | |||
Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease.,Gaur V, Wyatt HD, Komorowska W, Szczepanowski RH, de Sanctis D, Gorecka KM, West SC, Nowotny M Cell Rep. 2015 Mar 3. pii: S2211-1247(15)00165-5. doi:, 10.1016/j.celrep.2015.02.019. PMID:25753413<ref>PMID:25753413</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Gaur | <div class="pdbe-citations 4xlg" style="background-color:#fffaf0;"></div> | ||
[[Category: Gorecka | |||
[[Category: | ==See Also== | ||
[[Category: | *[[Endonuclease 3D structures|Endonuclease 3D structures]] | ||
[[Category: | == References == | ||
[[Category: West | <references/> | ||
[[Category: Wyatt | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Gaur V]] | |||
[[Category: Gorecka KM]] | |||
[[Category: Komorowska W]] | |||
[[Category: Nowotny M]] | |||
[[Category: Szczepanowski RH]] | |||
[[Category: West SC]] | |||
[[Category: Wyatt HDM]] | |||
[[Category: De Sanctis D]] | |||
Latest revision as of 13:49, 10 January 2024
C. glabrata Slx1 in complex with Slx4CCD.C. glabrata Slx1 in complex with Slx4CCD.
Structural highlights
FunctionSLX4_CANGA Regulatory subunit of the SLX1-SLX4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Publication Abstract from PubMedThe SLX1-SLX4 endonuclease required for homologous recombination and DNA repair in eukaryotic cells cleaves a variety of branched DNA structures. The nuclease subunit SLX1 is activated by association with a scaffolding protein SLX4. At the present time, little is known about the structure of SLX1-SLX4 or its mechanism of action. Here, we report the structural insights into SLX1-SLX4 by detailing the crystal structure of Candida glabrata (Cg) Slx1 alone and in combination with the C-terminal region of Slx4. The structure of Slx1 reveals a compact arrangement of the GIY-YIG nuclease and RING domains, which is reinforced by a long alpha helix. Slx1 forms a stable homodimer that blocks its active site. Slx1-Slx4 interaction is mutually exclusive with Slx1 homodimerization, suggesting a mechanism for Slx1 activation by Slx4. Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease.,Gaur V, Wyatt HD, Komorowska W, Szczepanowski RH, de Sanctis D, Gorecka KM, West SC, Nowotny M Cell Rep. 2015 Mar 3. pii: S2211-1247(15)00165-5. doi:, 10.1016/j.celrep.2015.02.019. PMID:25753413[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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