View source for 5zcz


==Solution structure of the T. Thermophilus HB8 TTHA1718 protein in living eukaryotic cells by in-cell NMR spectroscopy==
<StructureSection load='5zcz' size='340' side='right'caption='[[5zcz]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zcz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZCZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=5zcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zcz OCA], [https://pdbe.org/5zcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zcz RCSB], [https://www.ebi.ac.uk/pdbsum/5zcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zcz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q5SHL2_THET8 Q5SHL2_THET8] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteins in living cells interact specifically or nonspecifically with an enormous number of biomolecules. To understand the behavior of proteins under intracellular crowding conditions, it is indispensable to observe their three-dimensional (3D) structures at the atomic level in a physiologically natural environment. We demonstrate the first de novo protein structure determinations in eukaryotes with the sf9 cell/baculovirus system using NMR data from living cells exclusively. The method was applied to five proteins, rat calmodulin, human HRas, human ubiquitin, T. thermophilus HB8 TTHA1718, and Streptococcus protein G B1 domain. In all cases, we could obtain structural information from well-resolved in-cell 3D nuclear Overhauser effect spectroscopy (NOESY) data, suggesting that our method can be a standard tool for protein structure determinations in living eukaryotic cells. For three proteins, we achieved well-converged 3D structures. Among these, the in-cell structure of protein G B1 domain was most accurately determined, demonstrating that a helix-loop region is tilted away from a beta-sheet compared to the conformation in diluted solution.

High-Resolution Protein 3D Structure Determination in Living Eukaryotic Cells.,Tanaka T, Ikeya T, Kamoshida H, Suemoto Y, Mishima M, Shirakawa M, Guntert P, Ito Y Angew Chem Int Ed Engl. 2019 May 27;58(22):7284-7288. doi:, 10.1002/anie.201900840. Epub 2019 Apr 25. PMID:30938016<ref>PMID:30938016</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zcz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus HB8]]
[[Category: Guentert P]]
[[Category: Ito Y]]
[[Category: Kamoshida H]]
[[Category: Mishima M]]
[[Category: Shirakawa M]]
[[Category: Tanaka T]]
[[Category: Teppei I]]