2bx9: Difference between revisions
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== | ==Crystal structure of B.subtilis Anti-TRAP protein, an antagonist of TRAP-RNA interactions== | ||
In Bacillus subtilis the anti-TRAP protein (AT) is produced in response to | <StructureSection load='2bx9' size='340' side='right'caption='[[2bx9]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2bx9]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BX9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2bx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bx9 OCA], [https://pdbe.org/2bx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bx9 RCSB], [https://www.ebi.ac.uk/pdbsum/2bx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bx9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/RTPA_BACSU RTPA_BACSU] By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In Bacillus subtilis the anti-TRAP protein (AT) is produced in response to the accumulation of uncharged tRNA(Trp). AT regulates expression of genes involved in tryptophan biosynthesis and transport by binding to the tryptophan-activated trp RNA-binding attenuation protein (TRAP) and preventing its interaction with several mRNAs. Here, we report the x-ray structure of AT at 2.8 angstroms resolution, showing that the protein subunits assemble into tight trimers. Four such trimers are further associated into a 12-subunit particle in which individual trimers are related by twofold and threefold symmetry axes. Twelve DnaJ-like, cysteine-rich zinc-binding domains form spikes on the surface of the dodecamer. Available data suggest several possible ways for AT to interact with the 11-subunit TRAP. Interaction between the two symmetry-mismatching molecules could be assisted by the flexible nature of AT zinc-binding domains. | |||
Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction.,Shevtsov MB, Chen Y, Gollnick P, Antson AA Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17600-5. Epub 2005 Nov 23. PMID:16306262<ref>PMID:16306262</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2bx9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Antson | [[Category: Antson AA]] | ||
[[Category: Chen | [[Category: Chen Y]] | ||
[[Category: Gollnick | [[Category: Gollnick P]] | ||
[[Category: Shevtsov | [[Category: Shevtsov MB]] | ||
Latest revision as of 16:35, 30 August 2023
Crystal structure of B.subtilis Anti-TRAP protein, an antagonist of TRAP-RNA interactionsCrystal structure of B.subtilis Anti-TRAP protein, an antagonist of TRAP-RNA interactions
Structural highlights
FunctionRTPA_BACSU By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP. Publication Abstract from PubMedIn Bacillus subtilis the anti-TRAP protein (AT) is produced in response to the accumulation of uncharged tRNA(Trp). AT regulates expression of genes involved in tryptophan biosynthesis and transport by binding to the tryptophan-activated trp RNA-binding attenuation protein (TRAP) and preventing its interaction with several mRNAs. Here, we report the x-ray structure of AT at 2.8 angstroms resolution, showing that the protein subunits assemble into tight trimers. Four such trimers are further associated into a 12-subunit particle in which individual trimers are related by twofold and threefold symmetry axes. Twelve DnaJ-like, cysteine-rich zinc-binding domains form spikes on the surface of the dodecamer. Available data suggest several possible ways for AT to interact with the 11-subunit TRAP. Interaction between the two symmetry-mismatching molecules could be assisted by the flexible nature of AT zinc-binding domains. Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction.,Shevtsov MB, Chen Y, Gollnick P, Antson AA Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17600-5. Epub 2005 Nov 23. PMID:16306262[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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