3jsp
From Proteopedia
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| - | [[ | + | ==Classic Protein With a New Twist: crystal structure of a LexA repressor DNA complex== |
| + | <StructureSection load='3jsp' size='340' side='right' caption='[[3jsp]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3jsp]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JSP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JSP FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3jso|3jso]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lexA, exrA, spr, tsl, umuA, b4043, JW4003 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Repressor_lexA Repressor lexA], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.88 3.4.21.88] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3jsp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jsp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3jsp RCSB], [http://www.ebi.ac.uk/pdbsum/3jsp PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/js/3jsp_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:20703307</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Ecoli]] | |
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| - | == | + | |
| - | < | + | |
| - | [[Category: | + | |
[[Category: Repressor lexA]] | [[Category: Repressor lexA]] | ||
[[Category: Pigli, Y Z.]] | [[Category: Pigli, Y Z.]] | ||
Revision as of 09:46, 21 May 2014
Classic Protein With a New Twist: crystal structure of a LexA repressor DNA complex
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Categories: Ecoli | Repressor lexA | Pigli, Y Z. | Rice, P A. | Zhang, A P.P. | Autocatalytic cleavage | Dna damage | Dna repair | Dna replication | Dna-binding | Double helix | Hydrolase | Hydrolase-dna complex | Lexa | Protein-dna complex | Repressor | Sos response | Sos system | Transcription | Transcription regulation | Winged helix-turn-helix

