1kft

From Proteopedia

(Difference between revisions)

Revision as of 06:53, 11 August 2021

Solution Structure of the C-Terminal domain of UvrC from E-coli

Structural highlights

1kft is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UVRC_ECOLI] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The C-terminal domain of the UvrC protein (UvrC CTD) is essential for 5' incision in the prokaryotic nucleotide excision repair process. We have determined the three-dimensional structure of the UvrC CTD using heteronuclear NMR techniques. The structure shows two helix-hairpin-helix (HhH) motifs connected by a small connector helix. The UvrC CTD is shown to mediate structure-specific DNA binding. The domain binds to a single-stranded-double-stranded junction DNA, with a strong specificity towards looped duplex DNA that contains at least six unpaired bases per loop ("bubble DNA"). Using chemical shift perturbation experiments, the DNA-binding surface is mapped to the first hairpin region encompassing the conserved glycine-valine-glycine residues followed by lysine-arginine-arginine, a positively charged surface patch and the second hairpin region consisting of glycine-isoleucine-serine. A model for the protein-DNA complex is proposed that accounts for this specificity.

Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli.,Singh S, Folkers GE, Bonvin AM, Boelens R, Wechselberger R, Niztayev A, Kaptein R EMBO J. 2002 Nov 15;21(22):6257-66. PMID:12426397^[3]

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

References

↑ Lin JJ, Sancar A. Active site of (A)BC excinuclease. I. Evidence for 5' incision by UvrC through a catalytic site involving Asp399, Asp438, Asp466, and His538 residues. J Biol Chem. 1992 Sep 5;267(25):17688-92. PMID:1387639
↑ Verhoeven EE, van Kesteren M, Moolenaar GF, Visse R, Goosen N. Catalytic sites for 3' and 5' incision of Escherichia coli nucleotide excision repair are both located in UvrC. J Biol Chem. 2000 Feb 18;275(7):5120-3. PMID:10671556
↑ Singh S, Folkers GE, Bonvin AM, Boelens R, Wechselberger R, Niztayev A, Kaptein R. Solution structure and DNA-binding properties of the C-terminal domain of UvrC from E.coli. EMBO J. 2002 Nov 15;21(22):6257-66. PMID:12426397

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1kft"

@@ Line 3: / Line 3: @@
 <StructureSection load='1kft' size='340' side='right'caption='[[1kft]], [[NMR_Ensembles_of_Models | 22 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1kft]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KFT FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1kft]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFT FirstGlance]. <br>
-</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=1kft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kft OCA], [http://pdbe.org/1kft PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kft RCSB], [http://www.ebi.ac.uk/pdbsum/1kft PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kft ProSAT]</span></td></tr>
+</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=1kft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kft OCA], [https://pdbe.org/1kft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kft RCSB], [https://www.ebi.ac.uk/pdbsum/1kft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kft ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/UVRC_ECOLI UVRC_ECOLI]] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.<ref>PMID:1387639</ref> <ref>PMID:10671556</ref>
+[[https://www.uniprot.org/uniprot/UVRC_ECOLI UVRC_ECOLI]] The UvrABC repair system catalyzes the recognition and processing of DNA lesions. UvrC both incises the 5' and 3' sides of the lesion. The N-terminal half is responsible for the 3' incision and the C-terminal half is responsible for the 5' incision.<ref>PMID:1387639</ref> <ref>PMID:10671556</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1kft

From Proteopedia

Revision as of 06:53, 11 August 2021

Solution Structure of the C-Terminal domain of UvrC from E-coli

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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