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==C. glabrata Slx1 in complex with Slx4CCD.==
==C. glabrata Slx1 in complex with Slx4CCD.==
<StructureSection load='4xlg' size='340' side='right' caption='[[4xlg]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
<StructureSection load='4xlg' size='340' side='right'caption='[[4xlg]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4xlg]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XLG FirstGlance]. <br>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.78&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xlg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xlg OCA], [http://pdbe.org/4xlg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xlg RCSB], [http://www.ebi.ac.uk/pdbsum/4xlg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xlg 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>, <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>
</table>
== Function ==
== Function ==
[[http://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. [[http://www.uniprot.org/uniprot/SLX1_CANGA SLX1_CANGA]] Catalytic 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.  
[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;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 4xlg" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 4xlg" style="background-color:#fffaf0;"></div>
==See Also==
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Gaur, V]]
[[Category: Large Structures]]
[[Category: Gorecka, K M]]
[[Category: Gaur V]]
[[Category: Komorowska, W]]
[[Category: Gorecka KM]]
[[Category: Nowotny, M]]
[[Category: Komorowska W]]
[[Category: Sanctis, D de]]
[[Category: Nowotny M]]
[[Category: Szczepanowski, R H]]
[[Category: Szczepanowski RH]]
[[Category: West, S C]]
[[Category: West SC]]
[[Category: Wyatt, H D.M]]
[[Category: Wyatt HDM]]
[[Category: Dna repair]]
[[Category: De Sanctis D]]
[[Category: Giy-yig]]
[[Category: Homogolous recombination]]
[[Category: Hydrolase]]
[[Category: Nuclease]]

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

4xlg is a 2 chain structure with sequence from Candida glabrata CBS 138. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.78Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Gaur V, Wyatt HD, Komorowska W, Szczepanowski RH, de Sanctis D, Gorecka KM, West SC, Nowotny M. Structural and Mechanistic Analysis of the Slx1-Slx4 Endonuclease. Cell Rep. 2015 Mar 3. pii: S2211-1247(15)00165-5. doi:, 10.1016/j.celrep.2015.02.019. PMID:25753413 doi:http://dx.doi.org/10.1016/j.celrep.2015.02.019

4xlg, resolution 1.78Å

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OCA