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| | <StructureSection load='1gtf' size='340' side='right'caption='[[1gtf]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='1gtf' size='340' side='right'caption='[[1gtf]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gtf]] is a 23 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1GTF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gtf]] is a 23 chain structure with sequence from [https://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GTF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GTF FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c9s|1c9s]], [[1qaw|1qaw]]</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://proteopedia.org/fgij/fg.htm?mol=1gtf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtf OCA], [http://pdbe.org/1gtf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gtf RCSB], [http://www.ebi.ac.uk/pdbsum/1gtf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gtf 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=1gtf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gtf OCA], [https://pdbe.org/1gtf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gtf RCSB], [https://www.ebi.ac.uk/pdbsum/1gtf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gtf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/MTRB_GEOSE MTRB_GEOSE] |
| | == 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: Atcc 12980]] | + | [[Category: Geobacillus stearothermophilus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Antson, A A]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Gollnick, P]] | + | [[Category: Antson AA]] |
| - | [[Category: Hopcroft, N H]] | + | [[Category: Gollnick P]] |
| - | [[Category: Wendt, A L]] | + | [[Category: Hopcroft NH]] |
| - | [[Category: Rna binding protein-rna complex]] | + | [[Category: Wendt AL]] |
| - | [[Category: Rna-binding protein]]
| + | |
| - | [[Category: Transcription attenuation]]
| + | |
| - | [[Category: Trp rna]]
| + | |
| Structural highlights
Function
MTRB_GEOSE
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 trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes in bacilli by binding to the leader region of the nascent trp operon mRNA. When activated by binding tryptophan, the 11-subunit circular TRAP molecule binds to a target sequence consisting of 11 (G/U)AG repeats, separated by two or three variable 'spacer' nucleotides. Reported here are two crystal structures of TRAP bound to RNAs containing 11 GAG repeats separated by UU and CC spacer nucleotides, determined at 1.75 and 2.50 A resolution, respectively. These show the spacer regions of the RNA molecules to be highly flexible, making no direct hydrogen-bonding contacts with the protein. Comparison of these structures with the previous structure of TRAP bound to (GAGAU)(10)GAG RNA, in which the spacer nucleotides stack with each other close to the protein surface, shows that the RNA can adopt different conformations depending on the sequence of the spacer regions. This gives insight into the structural basis of the specificity of TRAP and into the mechanism of binding.
Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences.,Hopcroft NH, Wendt AL, Gollnick P, Antson AA Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):615-21. Epub 2002, Mar 22. PMID:11914485[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hopcroft NH, Wendt AL, Gollnick P, Antson AA. Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences. Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):615-21. Epub 2002, Mar 22. PMID:11914485
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