5lm7: Difference between revisions
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<StructureSection load='5lm7' size='340' side='right' caption='[[5lm7]], [[Resolution|resolution]] 3.35Å' scene=''> | <StructureSection load='5lm7' size='340' side='right' caption='[[5lm7]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5lm7]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LM7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LM7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5lm7]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteriophage_lambda Bacteriophage lambda], [http://en.wikipedia.org/wiki/Eco45 Eco45] and [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LM7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LM7 FirstGlance]. <br> | ||
</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=5lm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lm7 OCA], [http://pdbe.org/5lm7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lm7 RCSB], [http://www.ebi.ac.uk/pdbsum/5lm7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lm7 ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nusA, Z4530, ECs4050 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57]), nusB, ECS88_0411 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585035 ECO45]), rpsJ, ECS88_3708 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=585035 ECO45]), N, lambdap49 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10710 Bacteriophage lambda])</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=5lm7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lm7 OCA], [http://pdbe.org/5lm7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lm7 RCSB], [http://www.ebi.ac.uk/pdbsum/5lm7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lm7 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://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. [[http://www.uniprot.org/uniprot/NUSA_ECO57 NUSA_ECO57]] Participates in both transcription termination and antitermination. [[http://www.uniprot.org/uniprot/RS10_ECO45 RS10_ECO45]] Involved in the binding of tRNA to the ribosomes. [[http://www.uniprot.org/uniprot/NUSB_ECO45 NUSB_ECO45]] Involved in the transcription termination process. | [[http://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. [[http://www.uniprot.org/uniprot/NUSA_ECO57 NUSA_ECO57]] Participates in both transcription termination and antitermination. [[http://www.uniprot.org/uniprot/RS10_ECO45 RS10_ECO45]] Involved in the binding of tRNA to the ribosomes. [[http://www.uniprot.org/uniprot/NUSB_ECO45 NUSB_ECO45]] Involved in the transcription termination process. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
lambdaN-mediated processive antitermination constitutes a paradigmatic transcription regulatory event, during which phage protein lambdaN, host factors NusA, NusB, NusE and NusG, and an RNA nut site render elongating RNA polymerase termination-resistant. The structural basis of the process has so far remained elusive. Here we describe a crystal structure of a lambdaN-NusA-NusB-NusE-nut site complex and an electron cryo-microscopic structure of a complete transcription antitermination complex, comprising RNA polymerase, DNA, nut site RNA, all Nus factors and lambdaN, validated by crosslinking/mass spectrometry. Due to intrinsic disorder, lambdaN can act as a multiprotein/RNA interaction hub, which, together with nut site RNA, arranges NusA, NusB and NusE into a triangular complex. This complex docks via the NusA N-terminal domain and the lambdaN C-terminus next to the RNA exit channel on RNA polymerase. Based on the structures, comparative crosslinking analyses and structure-guided mutagenesis, we hypothesize that lambdaN mounts a multipronged strategy to reprogram the transcriptional machinery, which may include (1) the lambdaN C terminus clamping the RNA exit channel, thus stabilizing the DNA:RNA hybrid; (2) repositioning of NusA and RNAP elements, thus redirecting nascent RNA and sequestering the upstream branch of a terminator hairpin; and (3) hindering RNA engagement of termination factor rho and/or obstructing rho translocation on the transcript. | |||
Structural basis for lambdaN-dependent processive transcription antitermination.,Said N, Krupp F, Anedchenko E, Santos KF, Dybkov O, Huang YH, Lee CT, Loll B, Behrmann E, Burger J, Mielke T, Loerke J, Urlaub H, Spahn CMT, Weber G, Wahl MC Nat Microbiol. 2017 Apr 28;2:17062. doi: 10.1038/nmicrobiol.2017.62. PMID:28452979<ref>PMID:28452979</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5lm7" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacteriophage lambda]] | |||
[[Category: Eco45]] | |||
[[Category: Eco57]] | |||
[[Category: Said, N]] | [[Category: Said, N]] | ||
[[Category: Santos, K]] | [[Category: Santos, K]] | ||
Revision as of 10:39, 6 December 2017
Crystal structure of the lambda N-Nus factor complexCrystal structure of the lambda N-Nus factor complex
Structural highlights
Function[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. [NUSA_ECO57] Participates in both transcription termination and antitermination. [RS10_ECO45] Involved in the binding of tRNA to the ribosomes. [NUSB_ECO45] Involved in the transcription termination process. Publication Abstract from PubMedlambdaN-mediated processive antitermination constitutes a paradigmatic transcription regulatory event, during which phage protein lambdaN, host factors NusA, NusB, NusE and NusG, and an RNA nut site render elongating RNA polymerase termination-resistant. The structural basis of the process has so far remained elusive. Here we describe a crystal structure of a lambdaN-NusA-NusB-NusE-nut site complex and an electron cryo-microscopic structure of a complete transcription antitermination complex, comprising RNA polymerase, DNA, nut site RNA, all Nus factors and lambdaN, validated by crosslinking/mass spectrometry. Due to intrinsic disorder, lambdaN can act as a multiprotein/RNA interaction hub, which, together with nut site RNA, arranges NusA, NusB and NusE into a triangular complex. This complex docks via the NusA N-terminal domain and the lambdaN C-terminus next to the RNA exit channel on RNA polymerase. Based on the structures, comparative crosslinking analyses and structure-guided mutagenesis, we hypothesize that lambdaN mounts a multipronged strategy to reprogram the transcriptional machinery, which may include (1) the lambdaN C terminus clamping the RNA exit channel, thus stabilizing the DNA:RNA hybrid; (2) repositioning of NusA and RNAP elements, thus redirecting nascent RNA and sequestering the upstream branch of a terminator hairpin; and (3) hindering RNA engagement of termination factor rho and/or obstructing rho translocation on the transcript. Structural basis for lambdaN-dependent processive transcription antitermination.,Said N, Krupp F, Anedchenko E, Santos KF, Dybkov O, Huang YH, Lee CT, Loll B, Behrmann E, Burger J, Mielke T, Loerke J, Urlaub H, Spahn CMT, Weber G, Wahl MC Nat Microbiol. 2017 Apr 28;2:17062. doi: 10.1038/nmicrobiol.2017.62. PMID:28452979[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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