This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1wap
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1wap' size='340' side='right'caption='[[1wap]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1wap' size='340' side='right'caption='[[1wap]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1wap]] is a 22 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1wap]] is a 22 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=1WAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WAP 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]] 1.8Å</td></tr> |
| - | <tr id=' | + | <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'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wap OCA], [https://pdbe.org/1wap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wap RCSB], [https://www.ebi.ac.uk/pdbsum/1wap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wap ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/MTRB_BACSU MTRB_BACSU] Required for transcription attenuation control in the Trp operon. This trans-acting factor seems to recognize a 10 bases nucleotide sequence in the Trp leader transcript causing transcription termination. Binds the leader RNA only in presence of L-tryptophan.<ref>PMID:1551827</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 20: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wap ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wap ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of the trp RNA-binding attenuation protein of Bacclius subtilis solved at 1.8 A resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent beta-sheets in the beta-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan. | ||
| - | |||
| - | The structure of trp RNA-binding attenuation protein.,Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P Nature. 1995 Apr 20;374(6524):693-700. PMID:7715723<ref>PMID:7715723</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1wap" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
| Line 36: | Line 27: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bacillus subtilis]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Antson | + | [[Category: Antson AA]] |
| - | [[Category: Dodson | + | [[Category: Dodson EJ]] |
| - | [[Category: Gollnick | + | [[Category: Gollnick P]] |
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN
| |||||||||||
