7a4f: Difference between revisions
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<StructureSection load='7a4f' size='340' side='right'caption='[[7a4f]], [[Resolution|resolution]] 3.50Å' scene=''> | <StructureSection load='7a4f' size='340' side='right'caption='[[7a4f]], [[Resolution|resolution]] 3.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7a4f]] is a 120 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[7a4f]] is a 120 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus_VF5 Aquifex aeolicus VF5] 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=7A4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7A4F FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5Å</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=7a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a4f OCA], [https://pdbe.org/7a4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a4f RCSB], [https://www.ebi.ac.uk/pdbsum/7a4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a4f 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=7a4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7a4f OCA], [https://pdbe.org/7a4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7a4f RCSB], [https://www.ebi.ac.uk/pdbsum/7a4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7a4f ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/REGN_LAMBD REGN_LAMBD] Antitermination proteins positively regulate expression of the phage early and late gene operons. Bacterial host RNA polymerase modified by these antitermination proteins transcribes through termination sites that otherwise prevent expression of the regulated genes. N protein regulates the transition from the early to the middle stage of lytic development. It is a transcription antitermination protein that prevents termination at the rho-dependent tL and tR transcription termination sites.[https://www.uniprot.org/uniprot/RISB_AQUAE RISB_AQUAE] Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.<ref>PMID:12603336</ref> <ref>PMID:11237620</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aquifex aeolicus VF5]] | ||
[[Category: Escherichia virus Lambda]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hilvert | [[Category: Hilvert D]] | ||
[[Category: Tetter | [[Category: Tetter S]] | ||
Latest revision as of 10:43, 1 May 2024
Aquifex aeolicus lumazine synthase-derived nucleocapsid variant NC-1 (120-mer)Aquifex aeolicus lumazine synthase-derived nucleocapsid variant NC-1 (120-mer)
Structural highlights
FunctionREGN_LAMBD Antitermination proteins positively regulate expression of the phage early and late gene operons. Bacterial host RNA polymerase modified by these antitermination proteins transcribes through termination sites that otherwise prevent expression of the regulated genes. N protein regulates the transition from the early to the middle stage of lytic development. It is a transcription antitermination protein that prevents termination at the rho-dependent tL and tR transcription termination sites.RISB_AQUAE Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.[1] [2] References
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