3k3r

From Proteopedia

(Difference between revisions)

Revision as of 03:54, 25 December 2014

Unrefined crystal structure of a LexA-DNA complex

Structural highlights

3k3r is a 4 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3jso, 3jsp
Gene:	lexA, exrA, spr, tsl, umuA, b4043, JW4003 (Escherichia coli K-12)
Activity:	Repressor lexA, with EC number 3.4.21.88
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[LEXA_ECOLI] Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.^[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 eubacterial SOS system is a paradigm of cellular DNA damage and repair, and its activation can contribute to antibiotic resistance. Under normal conditions, LexA represses the transcription of many DNA repair proteins by binding to SOS 'boxes' in their operators. Under genotoxic stress, accumulating complexes of RecA, ATP and single-stranded DNA (ssDNA) activate LexA for autocleavage. To address how LexA recognizes its binding sites, we determined three crystal structures of Escherichia coli LexA in complex with SOS boxes. Here we report the structure of these LexA-DNA complexes. The DNA-binding domains of the LexA dimer interact with the DNA in the classical fashion of a winged helix-turn-helix motif. However, the wings of these two DNA-binding domains bind to the same minor groove of the DNA. These wing-wing contacts may explain why the spacing between the two half-sites of E. coli SOS boxes is invariant.

Structure of the LexA-DNA complex and implications for SOS box measurement.,Zhang AP, Pigli YZ, Rice PA Nature. 2010 Aug 12;466(7308):883-6. PMID:20703307^[3]

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

References

↑ Little JW, Mount DW, Yanisch-Perron CR. Purified lexA protein is a repressor of the recA and lexA genes. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4199-203. PMID:7027255
↑ Brent R, Ptashne M. Mechanism of action of the lexA gene product. Proc Natl Acad Sci U S A. 1981 Jul;78(7):4204-8. PMID:7027256
↑ Zhang AP, Pigli YZ, Rice PA. Structure of the LexA-DNA complex and implications for SOS box measurement. Nature. 2010 Aug 12;466(7308):883-6. PMID:20703307 doi:10.1038/nature09200

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3k3r"

@@ Line 8: / Line 8: @@
 <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=3k3r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k3r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k3r RCSB], [http://www.ebi.ac.uk/pdbsum/3k3r PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/LEXA_ECOLI LEXA_ECOLI]] Represses a number of genes involved in the response to DNA damage (SOS response), including recA and lexA. Binds to the 16 bp palindromic sequence 5'-CTGTATATATATACAG-3'. In the presence of single-stranded DNA, RecA interacts with LexA causing an autocatalytic cleavage which disrupts the DNA-binding part of LexA, leading to derepression of the SOS regulon and eventually DNA repair.<ref>PMID:7027255</ref> <ref>PMID:7027256</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3k3r

From Proteopedia

Revision as of 03:54, 25 December 2014

Unrefined crystal structure of a LexA-DNA complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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