View source for 5ef0


==RADIATION DAMAGE TO THE TRAP-RNA COMPLEX: DOSE (DWD) 16.7 MGy==
<StructureSection load='5ef0' size='340' side='right'caption='[[5ef0]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ef0]] is a 23 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EF0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5EF0 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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1gtf|1gtf]], [[5eeu|5eeu]]</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=5ef0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ef0 OCA], [http://pdbe.org/5ef0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ef0 RCSB], [http://www.ebi.ac.uk/pdbsum/5ef0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ef0 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Radiation damage during macromolecular X-ray crystallographic data collection is still the main impediment for many macromolecular structure determinations. Even when an eventual model results from the crystallographic pipeline, the manifestations of radiation-induced structural and conformation changes, the so-called specific damage, within crystalline macromolecules can lead to false interpretations of biological mechanisms. Although this has been well characterized within protein crystals, far less is known about specific damage effects within the larger class of nucleoprotein complexes. Here, a methodology has been developed whereby per-atom density changes could be quantified with increasing dose over a wide (1.3-25.0 MGy) range and at higher resolution (1.98 A) than the previous systematic specific damage study on a protein-DNA complex. Specific damage manifestations were determined within the large trp RNA-binding attenuation protein (TRAP) bound to a single-stranded RNA that forms a belt around the protein. Over a large dose range, the RNA was found to be far less susceptible to radiation-induced chemical changes than the protein. The availability of two TRAP molecules in the asymmetric unit, of which only one contained bound RNA, allowed a controlled investigation into the exact role of RNA binding in protein specific damage susceptibility. The 11-fold symmetry within each TRAP ring permitted statistically significant analysis of the Glu and Asp damage patterns, with RNA binding unexpectedly being observed to protect these otherwise highly sensitive residues within the 11 RNA-binding pockets distributed around the outside of the protein molecule. Additionally, the method enabled a quantification of the reduction in radiation-induced Lys and Phe disordering upon RNA binding directly from the electron density.

RNA protects a nucleoprotein complex against radiation damage.,Bury CS, McGeehan JE, Antson AA, Carmichael I, Gerstel M, Shevtsov MB, Garman EF Acta Crystallogr D Struct Biol. 2016 May 1;72(Pt 5):648-57. doi:, 10.1107/S2059798316003351. Epub 2016 Apr 26. PMID:27139628<ref>PMID:27139628</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5ef0" style="background-color:#fffaf0;"></div>

==See Also==
*[[Tryptophan RNA-binding attenuation protein|Tryptophan RNA-binding attenuation protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Bury, C S]]
[[Category: Garman, E F]]
[[Category: McGeehan, J E]]
[[Category: Shevtsov, M B]]
[[Category: Protein-rna complex]]
[[Category: Radiation damage]]
[[Category: Rna binding protein]]