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[[Image:2fco.gif|left|200px]]<br /><applet load="2fco" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2fco, resolution 1.40&Aring;" />
'''Crystal Structure of Bacillus stearothermophilus PrfA-Holliday Junction Resolvase'''<br />


==Overview==
==Crystal Structure of Bacillus stearothermophilus PrfA-Holliday Junction Resolvase==
Here we report a high resolution structure of RecU-Holliday junction resolvase from Bacillus stearothermophilus. The functional unit of RecU is a homodimer that contains a "mushroom" like structure with a rigid cap and two highly flexible loops extending outwards. These loops appear to be highly flexible/dynamic, and presumably are directly involved in DNA binding and holding it for catalysis. Structural modifications of both the protein and DNA upon their interaction are essential for catalysis. An Mg2+ ion is present in each of the two active sites in this homodimeric enzyme, and two water molecules are coordinated with each Mg2+ ion. Our data are consistent with one of these water molecules acting as a nucleophile and the other as a general acid. The identities of the general base and general acid involved in catalysis and the Lewis acid that stabilizes the pentacovalent transition state phosphate ion are proposed. A model for the RecU-Holliday junction DNA complex is also proposed and discussed in the context of DNA binding and cleavage.
<StructureSection load='2fco' size='340' side='right'caption='[[2fco]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fco]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_kaustophilus_HTA426 Geobacillus kaustophilus HTA426]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FCO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2fco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fco OCA], [https://pdbe.org/2fco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fco RCSB], [https://www.ebi.ac.uk/pdbsum/2fco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fco ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RECU_GEOKA RECU_GEOKA] Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.[HAMAP-Rule:MF_00130]<ref>PMID:12237459</ref>
== 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/fc/2fco_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/main_output.php?pdb_ID=2fco ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2FCO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_kaustophilus Geobacillus kaustophilus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Crossover_junction_endodeoxyribonuclease Crossover junction endodeoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.22.4 3.1.22.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCO OCA].
*[[Resolvase 3D structures|Resolvase 3D structures]]
 
== References ==
==Reference==
<references/>
Structure, flexibility, and mechanism of the Bacillus stearothermophilus RecU Holliday junction resolvase., Kelly SJ, Li J, Setlow P, Jedrzejas MJ, Proteins. 2007 Sep 1;68(4):961-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17557334 17557334]
__TOC__
[[Category: Crossover junction endodeoxyribonuclease]]
</StructureSection>
[[Category: Geobacillus kaustophilus]]
[[Category: Geobacillus kaustophilus HTA426]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Jedrzejas, M J.]]
[[Category: Jedrzejas MJ]]
[[Category: Li, J.]]
[[Category: Li J]]
[[Category: EDO]]
[[Category: MG]]
[[Category: crystal structure]]
[[Category: flexibility]]
[[Category: hydrolase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:20:02 2008''

Latest revision as of 12:22, 14 February 2024

Crystal Structure of Bacillus stearothermophilus PrfA-Holliday Junction ResolvaseCrystal Structure of Bacillus stearothermophilus PrfA-Holliday Junction Resolvase

Structural highlights

2fco is a 2 chain structure with sequence from Geobacillus kaustophilus HTA426. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RECU_GEOKA Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation.[HAMAP-Rule:MF_00130][1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Rigden DJ, Setlow P, Setlow B, Bagyan I, Stein RA, Jedrzejas MJ. PrfA protein of Bacillus species: prediction and demonstration of endonuclease activity on DNA. Protein Sci. 2002 Oct;11(10):2370-81. PMID:12237459 doi:10.1110/ps.0216802

2fco, resolution 1.40Å

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