4q0r

From Proteopedia

(Difference between revisions)

Revision as of 07:39, 8 February 2023

The catalytic core of Rad2 (complex I)

Structural highlights

4q0r is a 3 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RAD2_YEAST Single-stranded DNA endonuclease involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Essential for the incision step of excision-repair.^[1]

Publication Abstract from PubMed

Rad2/XPG belongs to the flap nuclease family and is responsible for a key step of the eukaryotic nucleotide excision DNA repair (NER) pathway. To elucidate the mechanism of DNA binding by Rad2/XPG, we solved crystal structures of the catalytic core of Rad2 in complex with a substrate. Rad2 utilizes three structural modules for recognition of the double-stranded portion of DNA substrate, particularly a Rad2-specific alpha-helix for binding the cleaved strand. The protein does not specifically recognize the single-stranded portion of the nucleic acid. Our data suggest that in contrast to related enzymes (FEN1 and EXO1), the Rad2 active site may be more accessible, which would create an exit route for substrates without a free 5' end.

Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.,Mietus M, Nowak E, Jaciuk M, Kustosz P, Studnicka J, Nowotny M Nucleic Acids Res. 2014 Aug 12. pii: gku729. PMID:25120270^[2]

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

References

↑ Habraken Y, Sung P, Prakash L, Prakash S. Yeast excision repair gene RAD2 encodes a single-stranded DNA endonuclease. Nature. 1993 Nov 25;366(6453):365-8. PMID:8247134 doi:http://dx.doi.org/10.1038/366365a0
↑ Mietus M, Nowak E, Jaciuk M, Kustosz P, Studnicka J, Nowotny M. Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding. Nucleic Acids Res. 2014 Aug 12. pii: gku729. PMID:25120270 doi:http://dx.doi.org/10.1093/nar/gku729

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4q0r"

@@ Line 3: / Line 3: @@
 <StructureSection load='4q0r' size='340' side='right'caption='[[4q0r]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4q0r]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q0R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q0R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4q0r]] is a 3 chain structure with sequence from [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=4Q0R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q0R FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q0w|4q0w]], [[4q0z|4q0z]], [[4q10|4q10]]</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=4q0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0r OCA], [https://pdbe.org/4q0r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q0r RCSB], [https://www.ebi.ac.uk/pdbsum/4q0r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0r ProSAT]</span></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=4q0r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q0r OCA], [http://pdbe.org/4q0r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q0r RCSB], [http://www.ebi.ac.uk/pdbsum/4q0r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q0r ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RAD2_YEAST RAD2_YEAST]] Single-stranded DNA endonuclease involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Essential for the incision step of excision-repair.<ref>PMID:8247134</ref>
+[https://www.uniprot.org/uniprot/RAD2_YEAST RAD2_YEAST] Single-stranded DNA endonuclease involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Essential for the incision step of excision-repair.<ref>PMID:8247134</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 23: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Jaciuk, M]]
+[[Category: Saccharomyces cerevisiae S288C]]
-[[Category: Kustosz, P]]
+[[Category: Jaciuk M]]
-[[Category: Mietus, M]]
+[[Category: Kustosz P]]
-[[Category: Nowak, E]]
+[[Category: Mietus M]]
-[[Category: Nowotny, M]]
+[[Category: Nowak E]]
-[[Category: Hydrolase-dna complex]]
+[[Category: Nowotny M]]
-[[Category: Nuclease]]
-[[Category: Nucleotide excision repair]]
-[[Category: Nucleus]]

4q0r

From Proteopedia

Revision as of 07:39, 8 February 2023

The catalytic core of Rad2 (complex I)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox