1flo: Difference between revisions

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<StructureSection load='1flo' size='340' side='right'caption='[[1flo]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='1flo' size='340' side='right'caption='[[1flo]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1flo]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1FLO FirstGlance]. <br>
<table><tr><td colspan='2'>[[1flo]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FLO FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene></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]] 2.65&#8491;</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHS:PHOSPHONIC+ACID'>PHS</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1flo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flo OCA], [http://pdbe.org/1flo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1flo RCSB], [http://www.ebi.ac.uk/pdbsum/1flo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1flo ProSAT]</span></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=1flo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flo OCA], [https://pdbe.org/1flo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1flo RCSB], [https://www.ebi.ac.uk/pdbsum/1flo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1flo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/FLP_YEAST 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.<ref>PMID:2040639</ref> <ref>PMID:3316982</ref> <ref>PMID:2254930</ref>
[https://www.uniprot.org/uniprot/FLP_YEAST 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.<ref>PMID:2040639</ref> <ref>PMID:3316982</ref> <ref>PMID:2254930</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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/main_output.php?pdb_ID=1flo ConSurf].
</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/main_output.php?pdb_ID=1flo ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a Flp recombinase tetramer bound to a Holliday junction intermediate has been determined at 2.65 A resolution. Only one of Flp's two domains, containing the active site, is structurally related to other lambda integrase family site-specific recombinases, such as Cre. The Flp active site differs, however, in that the helix containing the nucleophilic tyrosine is domain swapped, such that it cuts its DNA target in trans. The Flp tetramer displays pseudo four-fold symmetry matching that of the square planar Holliday junction substrate. This tetramer is stabilized by additional novel trans interactions among monomers. The structure illustrates how mechanistic unity is maintained on a chemical level while allowing for substantial variation on the structural level within a family of enzymes.
Crystal structure of a Flp recombinase-Holliday junction complex: assembly of an active oligomer by helix swapping.,Chen Y, Narendra U, Iype LE, Cox MM, Rice PA Mol Cell. 2000 Oct;6(4):885-97. PMID:11090626<ref>PMID:11090626</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1flo" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 18824]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, Y]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Cox, M M]]
[[Category: Chen Y]]
[[Category: Iype, L E]]
[[Category: Cox MM]]
[[Category: Narendra, U]]
[[Category: Iype LE]]
[[Category: Rice, P A]]
[[Category: Narendra U]]
[[Category: Domain-swapping]]
[[Category: Rice PA]]
[[Category: Holliday-junction]]
[[Category: Ligase]]
[[Category: Lyase-dna complex]]
[[Category: Protein-dna complex]]
[[Category: Tyrosine recombinase]]

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