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| | <StructureSection load='6p0t' size='340' side='right'caption='[[6p0t]], [[Resolution|resolution]] 3.60Å' scene=''> | | <StructureSection load='6p0t' size='340' side='right'caption='[[6p0t]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6p0t]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda] and [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6P0T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6p0t]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli], [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Escherichia_virus_Lambda Escherichia virus Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P0T FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fis, b3261, JW3229 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI]), xis ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.603Å</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=6p0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p0t OCA], [http://pdbe.org/6p0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6p0t RCSB], [http://www.ebi.ac.uk/pdbsum/6p0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6p0t 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=6p0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p0t OCA], [https://pdbe.org/6p0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p0t RCSB], [https://www.ebi.ac.uk/pdbsum/6p0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p0t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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. [[http://www.uniprot.org/uniprot/FIS_ECOLI FIS_ECOLI]] Activates ribosomal RNA transcription, as well other genes. Plays a direct role in upstream activation of rRNA promoters. Binds to a recombinational enhancer sequence that is required to stimulate hin-mediated DNA inversion. Prevents initiation of DNA replication from oriC.<ref>PMID:2209559</ref> <ref>PMID:8836178</ref> | + | [https://www.uniprot.org/uniprot/FIS_ECOLI FIS_ECOLI] Activates ribosomal RNA transcription, as well other genes. Plays a direct role in upstream activation of rRNA promoters. Binds to a recombinational enhancer sequence that is required to stimulate hin-mediated DNA inversion. Prevents initiation of DNA replication from oriC.<ref>PMID:2209559</ref> <ref>PMID:8836178</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: Bacteriophage lambda]] | + | [[Category: Escherichia coli]] |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | + | [[Category: Escherichia virus Lambda]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cascio, D]] | + | [[Category: Cascio D]] |
| - | [[Category: Hancock, S P]] | + | [[Category: Hancock SP]] |
| - | [[Category: Johnson, R C]] | + | [[Category: Johnson RC]] |
| - | [[Category: Cooperative binding]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Dna binding protein-dna complex]]
| + | |
| - | [[Category: Dna shape]]
| + | |
| - | [[Category: Protein-dna ternary complex]]
| + | |
| Structural highlights
Function
FIS_ECOLI Activates ribosomal RNA transcription, as well other genes. Plays a direct role in upstream activation of rRNA promoters. Binds to a recombinational enhancer sequence that is required to stimulate hin-mediated DNA inversion. Prevents initiation of DNA replication from oriC.[1] [2]
Publication Abstract from PubMed
Localized arrays of proteins cooperatively assemble onto chromosomes to control DNA activity in many contexts. Binding cooperativity is often mediated by specific protein-protein interactions, but cooperativity through DNA structure is becoming increasingly recognized as an additional mechanism. During the site-specific DNA recombination reaction that excises phage lambda from the chromosome, the bacterial DNA architectural protein Fis recruits multiple lambda-encoded Xis proteins to the attR recombination site. Here, we report X-ray crystal structures of DNA complexes containing Fis + Xis, which show little, if any, contacts between the two proteins. Comparisons with structures of DNA complexes containing only Fis or Xis, together with mutant protein and DNA binding studies, support a mechanism for cooperative protein binding solely by DNA allostery. Fis binding both molds the minor groove to potentiate insertion of the Xis beta-hairpin wing motif and bends the DNA to facilitate Xis-DNA contacts within the major groove. The Fis-structured minor groove shape that is optimized for Xis binding requires a precisely positioned pyrimidine-purine base-pair step, whose location has been shown to modulate minor groove widths in Fis-bound complexes to different DNA targets.
Cooperative DNA binding by proteins through DNA shape complementarity.,Hancock SP, Cascio D, Johnson RC Nucleic Acids Res. 2019 Sep 19;47(16):8874-8887. doi: 10.1093/nar/gkz642. PMID:31616952[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ross W, Thompson JF, Newlands JT, Gourse RL. E.coli Fis protein activates ribosomal RNA transcription in vitro and in vivo. EMBO J. 1990 Nov;9(11):3733-42. PMID:2209559
- ↑ Wold S, Crooke E, Skarstad K. The Escherichia coli Fis protein prevents initiation of DNA replication from oriC in vitro. Nucleic Acids Res. 1996 Sep 15;24(18):3527-32. PMID:8836178
- ↑ Hancock SP, Cascio D, Johnson RC. Cooperative DNA binding by proteins through DNA shape complementarity. Nucleic Acids Res. 2019 Sep 19;47(16):8874-8887. doi: 10.1093/nar/gkz642. PMID:31616952 doi:http://dx.doi.org/10.1093/nar/gkz642
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