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| | <StructureSection load='4m6f' size='340' side='right'caption='[[4m6f]], [[Resolution|resolution]] 4.99Å' scene=''> | | <StructureSection load='4m6f' size='340' side='right'caption='[[4m6f]], [[Resolution|resolution]] 4.99Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4m6f]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_mu Enterobacteria phage mu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4M6F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4m6f]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Mu Escherichia virus Mu] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M6F FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uj3|3uj3]], [[1gdt|1gdt]], [[3pkz|3pkz]]</td></tr> | + | </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=4m6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m6f OCA], [https://pdbe.org/4m6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m6f RCSB], [https://www.ebi.ac.uk/pdbsum/4m6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m6f ProSAT]</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=4m6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m6f OCA], [http://pdbe.org/4m6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m6f RCSB], [http://www.ebi.ac.uk/pdbsum/4m6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m6f ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DNIV_BPMU DNIV_BPMU]] This protein catalyzes the inversion of a 3000-bp segment of phage DNA. The inversion results in a modification of the 3'-end of the tail fiber gene and alters the host specificity. | + | [https://www.uniprot.org/uniprot/GIN_BPMU GIN_BPMU] Performs inversion of a viral 3 kp segment (G-segment) that encodes two alternate pairs of tail fiber proteins thereby modifying the host specificity of the virus. Binds as a dimer to the viral gix sites which are 34-bp palindromic sequences that flank the invertible G-segment. Catalyzes site-specific recombination in the presence of the host factor Fis. Gin dimers bound to each of the gix sites and host factor Fis bound to the enhancer come together to form the synaptic complex. Each Gin monomer introduces a nick and becomes covalently attached to the 5'-phosphate of the DNA, resulting in double-stranded staggered breaks at both recombination sites. A 180 degrees rotation of one of the two Gin dimers followed by religation of the DNA leads to the inversion of the G-segment (G+ or G- orientation).<ref>PMID:23275567</ref> <ref>PMID:2974801</ref> <ref>PMID:3159478</ref> <ref>PMID:6232613</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Enterobacteria phage mu]] | + | [[Category: Escherichia virus Mu]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ritacco, C J]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Steitz, T A]] | + | [[Category: Ritacco CJ]] |
| - | [[Category: Wang, J]] | + | [[Category: Steitz TA]] |
| - | [[Category: Catalytic domain]] | + | [[Category: Wang J]] |
| - | [[Category: Dna binding domain]]
| + | |
| - | [[Category: Helix-turn-helix]]
| + | |
| - | [[Category: Hydrolase-dna complex]]
| + | |
| - | [[Category: Recombinase]]
| + | |
| Structural highlights
Function
GIN_BPMU Performs inversion of a viral 3 kp segment (G-segment) that encodes two alternate pairs of tail fiber proteins thereby modifying the host specificity of the virus. Binds as a dimer to the viral gix sites which are 34-bp palindromic sequences that flank the invertible G-segment. Catalyzes site-specific recombination in the presence of the host factor Fis. Gin dimers bound to each of the gix sites and host factor Fis bound to the enhancer come together to form the synaptic complex. Each Gin monomer introduces a nick and becomes covalently attached to the 5'-phosphate of the DNA, resulting in double-stranded staggered breaks at both recombination sites. A 180 degrees rotation of one of the two Gin dimers followed by religation of the DNA leads to the inversion of the G-segment (G+ or G- orientation).[1] [2] [3] [4]
Publication Abstract from PubMed
Crystals of the G-segment invertase in complex with a 37-base-pair asymmetric DNA duplex substrate had an unusually high solvent content of 88% and diffracted to a maximal resolution of about 5.0 A. These crystals exhibited a high degree of non-isomorphism and anisotropy, which presented a serious challenge for structure determination by isomorphous replacement. Here, a procedure of cross-crystal averaging is described that uses large non-isomorphous crystallographic data with a priori information of an approximate molecular boundary as determined from a minimal amount of experimental phase information. Using this procedure, high-quality experimental phases were obtained that have enabled it to be shown that the conformation of the bound substrate DNA duplex significantly differs from those of substrates bound in other serine recombinase-DNA complexes.
Exploiting large non-isomorphous differences for phase determination of a G-segment invertase-DNA complex.,Ritacco CJ, Steitz TA, Wang J Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):685-93. doi:, 10.1107/S1399004713032392. Epub 2014 Feb 15. PMID:24598738[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ritacco CJ, Kamtekar S, Wang J, Steitz TA. Crystal structure of an intermediate of rotating dimers within the synaptic tetramer of the G-segment invertase. Nucleic Acids Res. 2013 Feb 1;41(4):2673-82. doi: 10.1093/nar/gks1303. Epub 2012 , Dec 28. PMID:23275567 doi:10.1093/nar/gks1303
- ↑ Klippel A, Cloppenborg K, Kahmann R. Isolation and characterization of unusual gin mutants. EMBO J. 1988 Dec 1;7(12):3983-9. doi: 10.1002/j.1460-2075.1988.tb03286.x. PMID:2974801 doi:http://dx.doi.org/10.1002/j.1460-2075.1988.tb03286.x
- ↑ Kahmann R, Rudt F, Koch C, Mertens G. G inversion in bacteriophage Mu DNA is stimulated by a site within the invertase gene and a host factor. Cell. 1985 Jul;41(3):771-80. doi: 10.1016/s0092-8674(85)80058-1. PMID:3159478 doi:http://dx.doi.org/10.1016/s0092-8674(85)80058-1
- ↑ Plasterk RH, Kanaar R, van de Putte P. A genetic switch in vitro: DNA inversion by Gin protein of phage Mu. Proc Natl Acad Sci U S A. 1984 May;81(9):2689-92. doi: 10.1073/pnas.81.9.2689. PMID:6232613 doi:http://dx.doi.org/10.1073/pnas.81.9.2689
- ↑ Ritacco CJ, Steitz TA, Wang J. Exploiting large non-isomorphous differences for phase determination of a G-segment invertase-DNA complex. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):685-93. doi:, 10.1107/S1399004713032392. Epub 2014 Feb 15. PMID:24598738 doi:http://dx.doi.org/10.1107/S1399004713032392
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