1u9l

From Proteopedia

(Difference between revisions)

Revision as of 07:25, 30 December 2020

Structural basis for a NusA- protein N interaction

Structural highlights

1u9l is a 3 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	nusA ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[NUSA_ECOLI] Participates in both transcription termination and antitermination. Involved in a variety of cellular and viral termination and antitermination processes, such as Rho-dependent transcriptional termination, intrinsic termination, and phage lambda N-mediated transcriptional antitermination. Also important for coordinating the cellular responses to DNA damage by coupling the processes of nucleotide excision repair and translesion synthesis to transcription.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The C terminus of transcription factor NusA from Escherichia coli comprises two repeat units, which bind during antitermination to protein N from phage lambda. To delineate the structural basis of the NusA-lambdaN interaction, we attempted to crystallize the NusA C-terminal repeats in complex with a lambdaN peptide (residues 34-47). The two NusA domains became proteolytically separated during crystallization, and crystals contained two copies of the first repeat unit in contact with a single lambdaN fragment. The NusA modules employ identical regions to contact the peptide but approach the ligand from opposite sides. In contrast to the alpha-helical conformation of the lambdaN N terminus in complex with boxB RNA, residues 34-40 of lambdaN remain extended upon interaction with NusA. Mutational analyses indicated that only one of the observed NusA-lambdaN interaction modes is biologically significant, supporting an equimolar ratio of NusA and lambdaN in antitermination complexes. Solution studies indicated that additional interactions are fostered by the second NusA repeat unit, consistent with known compensatory mutations in NusA and lambdaN. Contrary to the RNA polymerase alpha subunit, lambdaN binding does not stimulate RNA interaction of NusA. The results demonstrate that lambdaN serves as a scaffold to closely oppose NusA and the mRNA in antitermination complexes.

Structural basis for the interaction of Escherichia coli NusA with protein N of phage lambda.,Bonin I, Muhlberger R, Bourenkov GP, Huber R, Bacher A, Richter G, Wahl MC Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13762-7. Epub 2004 Sep 13. PMID:15365170^[10]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Greenblatt J, Li J. Interaction of the sigma factor and the nusA gene protein of E. coli with RNA polymerase in the initiation-termination cycle of transcription. Cell. 1981 May;24(2):421-8. PMID:6263495
↑ Greenblatt J, McLimont M, Hanly S. Termination of transcription by nusA gene protein of Escherichia coli. Nature. 1981 Jul 16;292(5820):215-20. PMID:6265785
↑ Schmidt MC, Chamberlin MJ. Amplification and isolation of Escherichia coli nusA protein and studies of its effects on in vitro RNA chain elongation. Biochemistry. 1984 Jan 17;23(2):197-203. PMID:6199039
↑ Schmidt MC, Chamberlin MJ. nusA protein of Escherichia coli is an efficient transcription termination factor for certain terminator sites. J Mol Biol. 1987 Jun 20;195(4):809-18. PMID:2821282 doi:http://dx.doi.org/10.1016/0022-2836(87)90486-4
↑ Liu K, Hanna MM. NusA contacts nascent RNA in Escherichia coli transcription complexes. J Mol Biol. 1995 Apr 7;247(4):547-58. PMID:7536848 doi:http://dx.doi.org/10.1006/jmbi.1994.0161
↑ Vogel U, Jensen KF. NusA is required for ribosomal antitermination and for modulation of the transcription elongation rate of both antiterminated RNA and mRNA. J Biol Chem. 1997 May 9;272(19):12265-71. PMID:9139668
↑ Gusarov I, Nudler E. Control of intrinsic transcription termination by N and NusA: the basic mechanisms. Cell. 2001 Nov 16;107(4):437-49. PMID:11719185
↑ Cohen SE, Lewis CA, Mooney RA, Kohanski MA, Collins JJ, Landick R, Walker GC. Roles for the transcription elongation factor NusA in both DNA repair and damage tolerance pathways in Escherichia coli. Proc Natl Acad Sci U S A. 2010 Aug 31;107(35):15517-22. doi:, 10.1073/pnas.1005203107. Epub 2010 Aug 9. PMID:20696893 doi:http://dx.doi.org/10.1073/pnas.1005203107
↑ Burmann BM, Rosch P. The role of E. coli Nus-factors in transcription regulation and transcription:translation coupling: From structure to mechanism. Transcription. 2011 May;2(3):130-134. PMID:21922055 doi:http://dx.doi.org/10.4161/trns.2.3.15671
↑ Bonin I, Muhlberger R, Bourenkov GP, Huber R, Bacher A, Richter G, Wahl MC. Structural basis for the interaction of Escherichia coli NusA with protein N of phage lambda. Proc Natl Acad Sci U S A. 2004 Sep 21;101(38):13762-7. Epub 2004 Sep 13. PMID:15365170 doi:10.1073/pnas.0405883101

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u9l"

@@ Line 1: / Line 1: @@
 ==Structural basis for a NusA- protein N interaction==
-<StructureSection load='1u9l' size='340' side='right' caption='[[1u9l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='1u9l' size='340' side='right'caption='[[1u9l]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1u9l]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1U9L FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1u9l]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U9L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1U9L FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU:GOLD+ION'>AU</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nusA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1u9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9l OCA], [http://pdbe.org/1u9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u9l RCSB], [http://www.ebi.ac.uk/pdbsum/1u9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u9l ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1u9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u9l OCA], [http://pdbe.org/1u9l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1u9l RCSB], [http://www.ebi.ac.uk/pdbsum/1u9l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1u9l ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 34: / Line 34: @@
 </StructureSection>
 [[Category: Bacillus coli migula 1895]]
+[[Category: Large Structures]]
 [[Category: Bacher, A]]
 [[Category: Bonin, I]]

1u9l

From Proteopedia

Revision as of 07:25, 30 December 2020

Structural basis for a NusA- protein N interaction

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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