1jhe

From Proteopedia

(Difference between revisions)

Revision as of 09:22, 17 January 2018

LEXA L89P Q92W E152A K156A MUTANT

Structural highlights

1jhe is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1jhc, 1jhf, 1jhh
Gene:	LexA ("Bacillus coli" Migula 1895)
Activity:	Repressor lexA, with EC number 3.4.21.88
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

LexA repressor undergoes a self-cleavage reaction. In vivo, this reaction requires an activated form of RecA, but it occurs spontaneously in vitro at high pH. Accordingly, LexA must both allow self-cleavage and yet prevent this reaction in the absence of a stimulus. We have solved the crystal structures of several mutant forms of LexA. Strikingly, two distinct conformations are observed, one compatible with cleavage, and the other in which the cleavage site is approximately 20 A from the catalytic center. Our analysis provides insight into the structural and energetic features that modulate the interconversion between these two forms and hence the rate of the self-cleavage reaction. We suggest RecA activates the self-cleavage of LexA and related proteins through selective stabilization of the cleavable conformation.

Crystal structure of LexA: a conformational switch for regulation of self-cleavage.,Luo Y, Pfuetzner RA, Mosimann S, Paetzel M, Frey EA, Cherney M, Kim B, Little JW, Strynadka NC Cell. 2001 Sep 7;106(5):585-94. PMID:11551506^[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
↑ Luo Y, Pfuetzner RA, Mosimann S, Paetzel M, Frey EA, Cherney M, Kim B, Little JW, Strynadka NC. Crystal structure of LexA: a conformational switch for regulation of self-cleavage. Cell. 2001 Sep 7;106(5):585-94. PMID:11551506

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/1jhe"

@@ Line 1: / Line 1: @@
 ==LEXA L89P Q92W E152A K156A MUTANT==
 <StructureSection load='1jhe' size='340' side='right' caption='[[1jhe]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LexA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
 <tr id='activity'><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 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=1jhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jhe OCA], [http://pdbe.org/1jhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jhe RCSB], [http://www.ebi.ac.uk/pdbsum/1jhe PDBsum]</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=1jhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jhe OCA], [http://pdbe.org/1jhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jhe RCSB], [http://www.ebi.ac.uk/pdbsum/1jhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jhe ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jh/1jhe_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jh/1jhe_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>

1jhe

From Proteopedia

Revision as of 09:22, 17 January 2018

LEXA L89P Q92W E152A K156A MUTANT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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