4dwl
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Avd molecule from Bordetella bacteriophage DGR== | |
| + | <StructureSection load='4dwl' size='340' side='right'caption='[[4dwl]], [[Resolution|resolution]] 2.69Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4dwl]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bordetella_virus_BPP1 Bordetella virus BPP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DWL 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]] 2.69Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4dwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dwl OCA], [https://pdbe.org/4dwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dwl RCSB], [https://www.ebi.ac.uk/pdbsum/4dwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dwl ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q775D7_BPBPP Q775D7_BPBPP] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Diversity-generating retroelements (DGRs) are the only known source of massive protein sequence variation in prokaryotes. These elements transfer coding information from a template region (TR) through an RNA intermediate to a protein-encoding variable region. This retrohoming process is accompanied by unique adenine-specific mutagenesis and, in the prototypical BPP-1 DGR, requires a reverse transcriptase (bRT) and an accessory variability determinant (bAvd) protein. To understand the role of bAvd, we determined its 2.69 A resolution structure, which revealed a highly positively charged pentameric barrel. In accordance with its charge, bAvd bound both DNA and RNA, albeit without a discernable sequence preference. We found that the coding sequence of bAvd functioned as part of TR but identified means to mutate bAvd without affecting TR. This mutational analysis revealed a strict correspondence between retrohoming and interaction of bAvd with bRT, suggesting that the bRT-bAvd complex is important for DGR retrohoming. | ||
| - | + | Structure of the essential diversity-generating retroelement protein bAvd and its functionally important interaction with reverse transcriptase.,Alayyoubi M, Guo H, Dey S, Golnazarian T, Brooks GA, Rong A, Miller JF, Ghosh P Structure. 2013 Feb 5;21(2):266-76. doi: 10.1016/j.str.2012.11.016. Epub 2012 Dec, 27. PMID:23273427<ref>PMID:23273427</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4dwl" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bordetella virus BPP1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Al-Ayyoubi M]] | ||
| + | [[Category: Ghosh P]] | ||
Current revision
Avd molecule from Bordetella bacteriophage DGR
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