View source for 5vf4


==Thermus aquaticus variable protein (TaqVP) from diversity-generating retroelements (DGR)==
<StructureSection load='5vf4' size='340' side='right'caption='[[5vf4]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5vf4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_aquaticus_Y51MC23 Thermus aquaticus Y51MC23]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VF4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VF4 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]] 2.81&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5vf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vf4 OCA], [https://pdbe.org/5vf4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vf4 RCSB], [https://www.ebi.ac.uk/pdbsum/5vf4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vf4 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Diversity-generating retroelements (DGRs) are widely distributed in bacteria, archaea, and microbial viruses, and bring about unparalleled levels of sequence variation in target proteins. While DGR variable proteins share low sequence identity, the structures of several such proteins have revealed the C-type lectin (CLec)-fold as a conserved scaffold for accommodating massive sequence variation. This conservation has led to the suggestion that the CLec-fold may be useful in molecular surface display applications. Thermostability is an attractive feature in such applications, and thus we studied the variable protein of a DGR encoded by a prophage of the thermophile Thermus aquaticus. We report here the 2.8 A resolution crystal structure of the variable protein from the T. aquaticus DGR, called TaqVP, and confirm that it has a CLec-fold. Remarkably, its variable region is nearly identical in structure to those of several other CLec-fold DGR variable proteins despite low sequence identity among these. TaqVP was found to be thermostable, which appears to be a property shared by several CLec-fold DGR variable proteins. These results provide impetus for the pursuit of the DGR variable protein CLec-fold in molecular display applications.

Crystal structure of a Thermus aquaticus diversity-generating retroelement variable protein.,Handa S, Shaw KL, Ghosh P PLoS One. 2019 Jan 10;14(1):e0205618. doi: 10.1371/journal.pone.0205618., eCollection 2019. PMID:30629599<ref>PMID:30629599</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5vf4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus aquaticus Y51MC23]]
[[Category: Ghosh P]]
[[Category: Handa S]]