4v4f: Difference between revisions

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New page: ==The structure of the trp RNA-binding attenuation protein (TRAP) bound to a RNA molecule containing UAGAU repeats== <StructureSection load='4v4f' size='340' side='right' caption='4v4f...
 
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==The structure of the trp RNA-binding attenuation protein (TRAP) bound to a RNA molecule containing UAGAU repeats==
==The structure of the trp RNA-binding attenuation protein (TRAP) bound to a RNA molecule containing UAGAU repeats==
<StructureSection load='4v4f' size='340' side='right' caption='[[4v4f]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4v4f' size='340' side='right'caption='[[4v4f]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4v4f]] is a 66 chain structure. This structure supersedes and combines the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1utf 1utf] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1utv 1utv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V4F FirstGlance]. <br>
<table><tr><td colspan='2'>[[4v4f]] is a 66 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1utf 1utf] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1utv 1utv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V4F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V4F FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1utf|1utf]], [[1utv|1utv]], [[1c9s|1c9s]], [[1gtf|1gtf]], [[1gtn|1gtn]], [[1qaw|1qaw]], [[1utd|1utd]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRP:TRYPTOPHAN'>TRP</scene></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=4v4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4v4f RCSB], [http://www.ebi.ac.uk/pdbsum/4v4f PDBsum]</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=4v4f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v4f OCA], [https://pdbe.org/4v4f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v4f RCSB], [https://www.ebi.ac.uk/pdbsum/4v4f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v4f ProSAT]</span></td></tr>
</table>
</table>
{{Large structure}}
== Function ==
[https://www.uniprot.org/uniprot/MTRB_GEOSE MTRB_GEOSE]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4v4f" style="background-color:#fffaf0;"></div>
==See Also==
*[[Tryptophan RNA-binding attenuation protein|Tryptophan RNA-binding attenuation protein]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Antson, A A]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Brzozowski, A M]]
[[Category: Large Structures]]
[[Category: Gollnick, P]]
[[Category: Synthetic construct]]
[[Category: Hopcroft, N H]]
[[Category: Antson AA]]
[[Category: Manfredo, A]]
[[Category: Brzozowski AM]]
[[Category: Wendt, A L]]
[[Category: Gollnick P]]
[[Category: Rna binding protein]]
[[Category: Hopcroft NH]]
[[Category: Rna-binding protein]]
[[Category: Manfredo A]]
[[Category: Transcription attenuation]]
[[Category: Wendt AL]]
[[Category: Trp rna]]

Latest revision as of 13:40, 10 January 2024

The structure of the trp RNA-binding attenuation protein (TRAP) bound to a RNA molecule containing UAGAU repeatsThe structure of the trp RNA-binding attenuation protein (TRAP) bound to a RNA molecule containing UAGAU repeats

Structural highlights

4v4f is a 66 chain structure with sequence from Geobacillus stearothermophilus and Synthetic construct. This structure supersedes the now removed PDB entries 1utf and 1utv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MTRB_GEOSE

Publication Abstract from PubMed

The trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes in several Bacilli by binding to the leader region of the nascent trp mRNA, inhibiting continued transcription. The 11 subunit TRAP molecule is active in complex with tryptophan, and binds consequently an RNA target segment consisting of 11 (G/U)AG triplets, each separated by two or three non-conserved "spacer" nucleotides. Here, we report the first crystal structures of TRAP in a complex with RNA containing UAG triplets separated by two nucleotides and in a complex with RNA containing GAG triplets separated by three nucleotides. Comparison with known structures of TRAP-RNA complexes shows that both substitution of G-1 with U-1 in the triplet and addition of an extra spacer nucleotide lead to a more flexible complex. This suggests an explanation why, in the trp leader RNA, all three-nucleotide spacer regions are followed by a G-1 nucleotide. Taken together, the structures demonstrate that RNA binding to TRAP is mediated by specific interactions involving the A-2 and G-3 nucleotides of the triplet. This is accompanied by the disruption of stacking interactions between the bases of the other nucleotides, contributing to the increase in entropy that drives binding.

The interaction of RNA with TRAP: the role of triplet repeats and separating spacer nucleotides.,Hopcroft NH, Manfredo A, Wendt AL, Brzozowski AM, Gollnick P, Antson AA J Mol Biol. 2004 Apr 16;338(1):43-53. PMID:15050822[1]

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

See Also

References

  1. Hopcroft NH, Manfredo A, Wendt AL, Brzozowski AM, Gollnick P, Antson AA. The interaction of RNA with TRAP: the role of triplet repeats and separating spacer nucleotides. J Mol Biol. 2004 Apr 16;338(1):43-53. PMID:15050822 doi:10.1016/j.jmb.2004.02.038

4v4f, resolution 1.90Å

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