1lx8: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (10 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein== | |||
<StructureSection load='1lx8' size='340' side='right'caption='[[1lx8]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1lx8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LX8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1lx8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lx8 OCA], [https://pdbe.org/1lx8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lx8 RCSB], [https://www.ebi.ac.uk/pdbsum/1lx8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lx8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/VXIS_LAMBD VXIS_LAMBD] Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
Upon induction of a bacteriophage lambda lysogen, a site-specific recombination reaction excises the phage genome from the chromosome of its bacterial host. A critical regulator of this process is the phage-encoded excisionase (Xis) protein, which functions both as a DNA architectural factor and by cooperatively recruiting integrase to an adjacent binding site specifically required for excision. Here we present the three-dimensional structure of Xis and the results of a structure-based mutagenesis study to define the molecular basis of its function. Xis adopts an unusual "winged"-helix motif that is modeled to interact with the major- and minor-grooves of its binding site through a single alpha-helix and loop structure ("wing"), respectively. The C-terminal tail of Xis, which is required for cooperative binding with integrase, is unstructured in the absence of DNA. We propose that asymmetric bending of DNA by Xis positions its unstructured C-terminal tail for direct contacts with the N-terminal DNA-binding domain of integrase and that an ensuing disordered to ordered transition of the tail may act to stabilize the formation of the tripartite integrase-Xis-DNA complex required for phage excision. | Upon induction of a bacteriophage lambda lysogen, a site-specific recombination reaction excises the phage genome from the chromosome of its bacterial host. A critical regulator of this process is the phage-encoded excisionase (Xis) protein, which functions both as a DNA architectural factor and by cooperatively recruiting integrase to an adjacent binding site specifically required for excision. Here we present the three-dimensional structure of Xis and the results of a structure-based mutagenesis study to define the molecular basis of its function. Xis adopts an unusual "winged"-helix motif that is modeled to interact with the major- and minor-grooves of its binding site through a single alpha-helix and loop structure ("wing"), respectively. The C-terminal tail of Xis, which is required for cooperative binding with integrase, is unstructured in the absence of DNA. We propose that asymmetric bending of DNA by Xis positions its unstructured C-terminal tail for direct contacts with the N-terminal DNA-binding domain of integrase and that an ensuing disordered to ordered transition of the tail may act to stabilize the formation of the tripartite integrase-Xis-DNA complex required for phage excision. | ||
Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein.,Sam MD, Papagiannis CV, Connolly KM, Corselli L, Iwahara J, Lee J, Phillips M, Wojciak JM, Johnson RC, Clubb RT J Mol Biol. 2002 Dec 6;324(4):791-805. PMID:12460578<ref>PMID:12460578</ref> | |||
Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein., Sam MD, Papagiannis CV, Connolly KM, Corselli L, Iwahara J, Lee J, Phillips M, Wojciak JM, Johnson RC, Clubb RT | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1lx8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia virus Lambda]] | |||
[[Category: Large Structures]] | |||
[[Category: Clubb RT]] | |||
[[Category: Connolly KM]] | |||
[[Category: Corselli L]] | |||
[[Category: Iwahara J]] | |||
[[Category: Johnson RC]] | |||
[[Category: Lee J]] | |||
[[Category: Papagiannis C]] | |||
[[Category: Phillips M]] | |||
[[Category: Sam MD]] | |||
[[Category: Wojciak JM]] | |||
Latest revision as of 14:23, 2 August 2023
Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis proteinRegulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein
Structural highlights
FunctionVXIS_LAMBD Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site. Publication Abstract from PubMedUpon induction of a bacteriophage lambda lysogen, a site-specific recombination reaction excises the phage genome from the chromosome of its bacterial host. A critical regulator of this process is the phage-encoded excisionase (Xis) protein, which functions both as a DNA architectural factor and by cooperatively recruiting integrase to an adjacent binding site specifically required for excision. Here we present the three-dimensional structure of Xis and the results of a structure-based mutagenesis study to define the molecular basis of its function. Xis adopts an unusual "winged"-helix motif that is modeled to interact with the major- and minor-grooves of its binding site through a single alpha-helix and loop structure ("wing"), respectively. The C-terminal tail of Xis, which is required for cooperative binding with integrase, is unstructured in the absence of DNA. We propose that asymmetric bending of DNA by Xis positions its unstructured C-terminal tail for direct contacts with the N-terminal DNA-binding domain of integrase and that an ensuing disordered to ordered transition of the tail may act to stabilize the formation of the tripartite integrase-Xis-DNA complex required for phage excision. Regulation of directionality in bacteriophage lambda site-specific recombination: structure of the Xis protein.,Sam MD, Papagiannis CV, Connolly KM, Corselli L, Iwahara J, Lee J, Phillips M, Wojciak JM, Johnson RC, Clubb RT J Mol Biol. 2002 Dec 6;324(4):791-805. PMID:12460578[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
| ||||||||||||||||