3imq: Difference between revisions
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<StructureSection load='3imq' size='340' side='right'caption='[[3imq]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3imq' size='340' side='right'caption='[[3imq]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3imq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3imq]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IMQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IMQ 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">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3imq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3imq OCA], [https://pdbe.org/3imq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3imq RCSB], [https://www.ebi.ac.uk/pdbsum/3imq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3imq 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=3imq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3imq OCA], [https://pdbe.org/3imq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3imq RCSB], [https://www.ebi.ac.uk/pdbsum/3imq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3imq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/NUSB_ECOLI NUSB_ECOLI] One of the proteins essential for the formation of the RNA polymerase antitermination complex in the presence of lambda phage N protein. However, it is involved in the transcription termination process at certain sites during normal bacterial growth. Binds to the BoxA RNA motif. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Luo | [[Category: Luo X]] | ||
[[Category: Wahl | [[Category: Wahl MC]] | ||
Latest revision as of 10:53, 6 September 2023
Crystal structure of the NusB101-S10(delta loop) complexCrystal structure of the NusB101-S10(delta loop) complex
Structural highlights
FunctionNUSB_ECOLI One of the proteins essential for the formation of the RNA polymerase antitermination complex in the presence of lambda phage N protein. However, it is involved in the transcription termination process at certain sites during normal bacterial growth. Binds to the BoxA RNA motif. 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 PubMedPhage lambda propagation in Escherichia coli host cells requires transcription antitermination on the lambda chromosome mediated by lambdaN protein and four host Nus factors, NusA, B, E (ribosomal S10) and G. Interaction of E. coli NusB:NusE heterodimer with the single stranded BoxA motif of lambdanutL or lambdanutR RNA is crucial for this reaction. Similarly, binding of NusB:NusE to a BoxA motif is essential to suppress transcription termination in the ribosomal RNA (rrn) operons. We used fluorescence anisotropy to measure the binding properties of NusB and of NusB:NusE heterodimer to BoxA-containing RNAs differing in length and sequence. Our results demonstrate that BoxA is necessary and sufficient for binding. We also studied the gain-of-function D118N NusB mutant that allows lambda growth in nusA1 or nusE71 mutants. In vivo lambda burst-size determinations, CD thermal unfolding measurements and X-ray crystallography of this as well as various other NusB D118 mutants showed the importance of size and polarity of amino acid 118 for RNA binding and other interactions. Our work suggests that the affinity of the NusB:NusE complex to BoxA RNA is precisely tuned to maximize control of transcription termination. Fine tuning of the E. coli NusB:NusE complex affinity to BoxA RNA is required for processive antitermination.,Burmann BM, Luo X, Rosch P, Wahl MC, Gottesman ME Nucleic Acids Res. 2010 Jan;38(1):314-26. Epub 2009 Oct 23. PMID:19854945[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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