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2nrr

From Proteopedia

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Current revision

Crystal structure of the C-terminal RNAseH endonuclase domain of UvrC

Structural highlights

2nrr is a 1 chain structure with sequence from Thermotoga maritima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UVRC_THEMA 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 (By similarity).

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

Removal and repair of DNA damage by the nucleotide excision repair pathway requires two sequential incision reactions, which are achieved by the endonuclease UvrC in eubacteria. Here, we describe the crystal structure of the C-terminal half of UvrC, which contains the catalytic domain responsible for 5' incision and a helix-hairpin-helix-domain that is implicated in DNA binding. Surprisingly, the 5' catalytic domain shares structural homology with RNase H despite the lack of sequence homology and contains an uncommon DDH triad. The structure also reveals two highly conserved patches on the surface of the protein, which are not related to the active site. Mutations of residues in one of these patches led to the inability of the enzyme to bind DNA and severely compromised both incision reactions. Based on our results, we suggest a model of how UvrC forms a productive protein-DNA complex to excise the damage from DNA.

Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad.,Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C EMBO J. 2007 Jan 24;26(2):613-22. PMID:17245438^[1]

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

References

↑ Karakas E, Truglio JJ, Croteau D, Rhau B, Wang L, Van Houten B, Kisker C. Structure of the C-terminal half of UvrC reveals an RNase H endonuclease domain with an Argonaute-like catalytic triad. EMBO J. 2007 Jan 24;26(2):613-22. PMID:17245438

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/2nrr"

Categories: Large Structures | Thermotoga maritima | Karakas E | Kisker C | Truglio JJ

@@ Line 3: / Line 3: @@
 <StructureSection load='2nrr' size='340' side='right'caption='[[2nrr]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2nrr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NRR FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2nrr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NRR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NRR FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ycz|1ycz]], [[1yd0|1yd0]], [[1yd1|1yd1]], [[1yd6|1yd6]], [[2nrt|2nrt]], [[2nrv|2nrv]], [[2nrw|2nrw]], [[2nrx|2nrx]], [[2nrz|2nrz]]</div></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]] 1.2&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">uvrC ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=2nrr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nrr OCA], [https://pdbe.org/2nrr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nrr RCSB], [https://www.ebi.ac.uk/pdbsum/2nrr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nrr ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/UVRC_THEMA UVRC_THEMA]] 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 (By similarity).
+[https://www.uniprot.org/uniprot/UVRC_THEMA UVRC_THEMA] 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 (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 43589]]
 [[Category: Large Structures]]
-[[Category: Karakas, E]]
+[[Category: Thermotoga maritima]]
-[[Category: Kisker, C]]
+[[Category: Karakas E]]
-[[Category: Truglio, J J]]
+[[Category: Kisker C]]
-[[Category: Endonuclase]]
+[[Category: Truglio JJ]]
-[[Category: Hydrolase]]
-[[Category: Ner]]
-[[Category: Uvrc]]

2nrr

From Proteopedia

Current revision

Crystal structure of the C-terminal RNAseH endonuclase domain of UvrC

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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