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| | ==Solution Structure of Full-Length Excisionase (Xis) from Bacteriophage HK022== | | ==Solution Structure of Full-Length Excisionase (Xis) from Bacteriophage HK022== |
| - | <StructureSection load='1pm6' size='340' side='right' caption='[[1pm6]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1pm6' size='340' side='right'caption='[[1pm6]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pm6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bphk0 Bphk0]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PM6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PM6 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pm6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_HK022 Escherichia virus HK022]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PM6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PM6 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">XIS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10742 BPHK0])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pm6 OCA], [http://pdbe.org/1pm6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pm6 RCSB], [http://www.ebi.ac.uk/pdbsum/1pm6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1pm6 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=1pm6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pm6 OCA], [https://pdbe.org/1pm6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pm6 RCSB], [https://www.ebi.ac.uk/pdbsum/1pm6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pm6 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/VXIS_BPHK0 VXIS_BPHK0]] Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site. | + | [https://www.uniprot.org/uniprot/VXIS_BPHK0 VXIS_BPHK0] 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bphk0]] | + | [[Category: Escherichia virus HK022]] |
| - | [[Category: Kleinhaus, I]] | + | [[Category: Large Structures]] |
| - | [[Category: Loehr, F]] | + | [[Category: Kleinhaus I]] |
| - | [[Category: Luecke, C]] | + | [[Category: Loehr F]] |
| - | [[Category: Muresanu, L]] | + | [[Category: Luecke C]] |
| - | [[Category: Pristovsek, P]] | + | [[Category: Muresanu L]] |
| - | [[Category: Rogov, V V]] | + | [[Category: Pristovsek P]] |
| - | [[Category: Rueterjans, H]] | + | [[Category: Rogov VV]] |
| - | [[Category: Werner, K]] | + | [[Category: Rueterjans H]] |
| - | [[Category: Wienk, H]] | + | [[Category: Werner K]] |
| - | [[Category: Antiparallel beta-sheet]]
| + | [[Category: Wienk H]] |
| - | [[Category: Cis-trans-trans triproline]]
| + | |
| - | [[Category: Gene regulation]]
| + | |
| - | [[Category: Winged-helix]]
| + | |
| Structural highlights
Function
VXIS_BPHK0 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 PubMed
Heteronuclear high-resolution NMR spectroscopy was employed to determine the solution structure of the excisionase protein (Xis) from the lambda-like bacteriophage HK022 and to study its sequence-specific DNA interaction. As wild-type Xis was previously characterized as a generally unstable protein, a biologically active HK022 Xis mutant with a single amino acid substitution Cys28-->Ser was used in this work. This substitution has been shown to diminish the irreversibility of Xis denaturation and subsequent degradation, but does not affect the structural or thermodynamic properties of the protein, as evidenced by NMR and differential scanning calorimetry. The solution structure of HK022 Xis forms a compact, highly ordered protein core with two well-defined alpha-helices (residues 5-11 and 18-27) and five beta-strands (residues 2-4, 30-31, 35-36, 41-44 and 48-49). These data correlate well with 1H2O-2H2O exchange experiments and imply a different organization of the HK022 Xis secondary structure elements in comparison with the previously determined structure of the bacteriophage lambda excisionase. Superposition of both Xis structures indicates a better correspondence of the full-length HK022 Xis to the typical 'winged-helix' DNA-binding motif, as found, for example, in the DNA-binding domain of the Mu-phage repressor. Residues 51-72, which were not resolved in the lambda Xis, do not show any regular structure in HK022 Xis and thus appear to be completely disordered in solution. The resonance assignments have shown, however, that an unusual connectivity exists between residues Asn66 and Gly67 owing to asparagine-isoaspartyl isomerization. Such an isomerization has been previously observed and characterized only in eukaryotic proteins.
Solution structure and stability of the full-length excisionase from bacteriophage HK022.,Rogov VV, Lucke C, Muresanu L, Wienk H, Kleinhaus I, Werner K, Lohr F, Pristovsek P, Ruterjans H Eur J Biochem. 2003 Dec;270(24):4846-58. PMID:14653811[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rogov VV, Lucke C, Muresanu L, Wienk H, Kleinhaus I, Werner K, Lohr F, Pristovsek P, Ruterjans H. Solution structure and stability of the full-length excisionase from bacteriophage HK022. Eur J Biochem. 2003 Dec;270(24):4846-58. PMID:14653811
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