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1m6x

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Revision as of 08:04, 31 January 2018

Flpe-Holliday Junction Complex

Structural highlights

1m6x is a 10 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1flo
Gene:	FLP1 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[FLP_YEAST] Part of the plasmid amplification system, which corrects any decrease in copy number caused by a rare missegregation event. Catalyzes the recombination between the large inverted repetitions of the 2-micron plasmid during plasmid replication. This recombination event changes the direction of one of the two replication forks in the bidirectionally replicating molecule, effectively resulting in multiple rounds of replication from a single initiation event. Binds specifically to the FLP recognition target (FRT) site where it induces DNA to bend. Three types of bend exist. Type I is approximately 60 degrees and results from 1 FLP molecule binding to 1 symmetry element. Type II is >144 degrees and results from FLP molecules binding to symmetry elements a and b. Type III is approximately 65 degrees and results from FLP molecules binding to symmetry elements b and c.^[1] ^[2] ^[3]

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 Flp recombinase, a member of the lambda integrase or tyrosine-based family of site-specific recombinases, is an interesting example of an enzyme whose catalytic activity is regulated by protein-protein contacts. It exhibits half-of-the-sites activity throughout its catalytic cycle. Flp is unique among these recombinases, in that it assembles each active site in trans through the interaction of two protein monomers within the catalytic tetramer, with isomerization of interacting pairs being essential to complete a full reaction. We report here the structure of a DNA-bound tetramer of Flpe, a variant of Flp that is more active at 37 degrees C than the wild-type recombinase. This new structure includes the first observation of a tyrosine recombinase with an invading 5'-OH poised to attack the covalent phosphotyrosine residue. Comparison with the previously determined Flp structure highlights differences in flexibility between the two types of protein-protein interfaces in the tetramer and better defines the range of conformations available to this remarkably flexible complex. These results suggest a steric occlusion model for enforcement of half-of-the-sites activity.

Structural plasticity of the Flp-Holliday junction complex.,Conway AB, Chen Y, Rice PA J Mol Biol. 2003 Feb 14;326(2):425-34. PMID:12559911^[4]

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

References

↑ Pan H, Clary D, Sadowski PD. Identification of the DNA-binding domain of the FLP recombinase. J Biol Chem. 1991 Jun 15;266(17):11347-54. PMID:2040639
↑ Reynolds AE, Murray AW, Szostak JW. Roles of the 2 microns gene products in stable maintenance of the 2 microns plasmid of Saccharomyces cerevisiae. Mol Cell Biol. 1987 Oct;7(10):3566-73. PMID:3316982
↑ Schwartz CJ, Sadowski PD. FLP protein of 2 mu circle plasmid of yeast induces multiple bends in the FLP recognition target site. J Mol Biol. 1990 Nov 20;216(2):289-98. PMID:2254930
↑ Conway AB, Chen Y, Rice PA. Structural plasticity of the Flp-Holliday junction complex. J Mol Biol. 2003 Feb 14;326(2):425-34. PMID:12559911

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/1m6x"

@@ Line 1: / Line 1: @@
 ==Flpe-Holliday Junction Complex==
 <StructureSection load='1m6x' size='340' side='right' caption='[[1m6x]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1flo|1flo]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FLP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1m6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6x OCA], [http://pdbe.org/1m6x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m6x RCSB], [http://www.ebi.ac.uk/pdbsum/1m6x 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=1m6x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m6x OCA], [http://pdbe.org/1m6x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m6x RCSB], [http://www.ebi.ac.uk/pdbsum/1m6x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m6x 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/m6/1m6x_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m6/1m6x_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1m6x" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Resolvase|Resolvase]]
 == References ==
 <references/>

1m6x

From Proteopedia

Revision as of 08:04, 31 January 2018

Flpe-Holliday Junction Complex

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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