2hoi: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2hoi.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2hoi", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2hoi|  PDB=2hoi  |  SCENE=  }}
'''Crystal structure of the tetrameric pre-cleavage synaptic complex in the cre-loxp site-specific recombination'''


==Crystal structure of the tetrameric pre-cleavage synaptic complex in the cre-loxp site-specific recombination==
<StructureSection load='2hoi' size='340' side='right'caption='[[2hoi]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2hoi]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_P1 Escherichia virus P1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HOI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HOI 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]] 2.601&#8491;</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=2hoi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hoi OCA], [https://pdbe.org/2hoi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hoi RCSB], [https://www.ebi.ac.uk/pdbsum/2hoi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hoi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RECR_BPP1 RECR_BPP1] Catalyzes site-specific recombination between two 34-base-pair LOXP sites. Its role is to maintain the phage genome as a monomeric unit-copy plasmid in the lysogenic state.
== 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/ho/2hoi_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=2hoi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cre recombinase catalyzes site-specific recombination between 34-bp loxP sites in a variety of topological and cellular contexts. An obligatory step in the recombination reaction is the association, or synapsis, of Cre-bound loxP sites to form a tetrameric protein assembly that is competent for strand exchange. Using analytical ultracentrifugation and electrophoresis approaches, we have studied the energetics of Cre-mediated synapsis of loxP sites. We found that synapsis occurs with a high affinity (Kd = 10 nM) and is pH-dependent but does not require divalent cations. Surprisingly, the catalytically inactive Cre K201A mutant is fully competent for synapsis of loxP sites, yet the inactive Y324F and R173K mutants are defective for synapsis. These findings have allowed us to determine the first crystal structures of a pre-cleavage Cre-loxP synaptic complex in a configuration representing the starting point in the recombination pathway. When combined with a quantitative analysis of synapsis using loxP mutants, the structures explain how the central 8 bp of the loxP site are able to dictate the order of strand exchange in the Cre system.


==Overview==
Synapsis of loxP sites by Cre recombinase.,Ghosh K, Guo F, Van Duyne GD J Biol Chem. 2007 Aug 17;282(33):24004-16. Epub 2007 Jun 15. PMID:17573343<ref>PMID:17573343</ref>
Cre recombinase catalyzes site-specific recombination between 34-bp loxP sites in a variety of topological and cellular contexts. An obligatory step in the recombination reaction is the association, or synapsis, of Cre-bound loxP sites to form a tetrameric protein assembly that is competent for strand exchange. Using analytical ultracentrifugation and electrophoresis approaches, we have studied the energetics of Cre-mediated synapsis of loxP sites. We found that synapsis occurs with a high affinity (Kd = 10 nM) and is pH-dependent but does not require divalent cations. Surprisingly, the catalytically inactive Cre K201A mutant is fully competent for synapsis of loxP sites, yet the inactive Y324F and R173K mutants are defective for synapsis. These findings have allowed us to determine the first crystal structures of a pre-cleavage Cre-loxP synaptic complex in a configuration representing the starting point in the recombination pathway. When combined with a quantitative analysis of synapsis using loxP mutants, the structures explain how the central 8 bp of the loxP site are able to dictate the order of strand exchange in the Cre system.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2HOI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p1 Enterobacteria phage p1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HOI OCA].
</div>
<div class="pdbe-citations 2hoi" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Synapsis of loxP sites by Cre recombinase., Ghosh K, Guo F, Van Duyne GD, J Biol Chem. 2007 Aug 17;282(33):24004-16. Epub 2007 Jun 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17573343 17573343]
*[[Resolvase 3D structures|Resolvase 3D structures]]
[[Category: Enterobacteria phage p1]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Duyne, G D.Van.]]
__TOC__
[[Category: Ghosh, K.]]
</StructureSection>
[[Category: Cre-loxp precleavage synapse]]
[[Category: Escherichia virus P1]]
[[Category: Recombination/dna complex]]
[[Category: Large Structures]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:31:11 2008''
[[Category: Ghosh K]]
[[Category: Van Duyne GD]]

Latest revision as of 13:00, 30 August 2023

Crystal structure of the tetrameric pre-cleavage synaptic complex in the cre-loxp site-specific recombinationCrystal structure of the tetrameric pre-cleavage synaptic complex in the cre-loxp site-specific recombination

Structural highlights

2hoi is a 8 chain structure with sequence from Escherichia virus P1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.601Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RECR_BPP1 Catalyzes site-specific recombination between two 34-base-pair LOXP sites. Its role is to maintain the phage genome as a monomeric unit-copy plasmid in the lysogenic state.

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

Cre recombinase catalyzes site-specific recombination between 34-bp loxP sites in a variety of topological and cellular contexts. An obligatory step in the recombination reaction is the association, or synapsis, of Cre-bound loxP sites to form a tetrameric protein assembly that is competent for strand exchange. Using analytical ultracentrifugation and electrophoresis approaches, we have studied the energetics of Cre-mediated synapsis of loxP sites. We found that synapsis occurs with a high affinity (Kd = 10 nM) and is pH-dependent but does not require divalent cations. Surprisingly, the catalytically inactive Cre K201A mutant is fully competent for synapsis of loxP sites, yet the inactive Y324F and R173K mutants are defective for synapsis. These findings have allowed us to determine the first crystal structures of a pre-cleavage Cre-loxP synaptic complex in a configuration representing the starting point in the recombination pathway. When combined with a quantitative analysis of synapsis using loxP mutants, the structures explain how the central 8 bp of the loxP site are able to dictate the order of strand exchange in the Cre system.

Synapsis of loxP sites by Cre recombinase.,Ghosh K, Guo F, Van Duyne GD J Biol Chem. 2007 Aug 17;282(33):24004-16. Epub 2007 Jun 15. PMID:17573343[1]

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

See Also

References

  1. ↑ Ghosh K, Guo F, Van Duyne GD. Synapsis of loxP sites by Cre recombinase. J Biol Chem. 2007 Aug 17;282(33):24004-16. Epub 2007 Jun 15. PMID:17573343 doi:10.1074/jbc.M703283200

2hoi, resolution 2.60Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2hoi&oldid=3851150"