View source for 7cph


==Crystal structure of tRNA adenosine deaminase from Bacillus subtilis==
<StructureSection load='7cph' size='340' side='right'caption='[[7cph]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7cph]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CPH 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7cph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7cph OCA], [https://pdbe.org/7cph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7cph RCSB], [https://www.ebi.ac.uk/pdbsum/7cph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7cph ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TADA_BACSU TADA_BACSU] Catalyzes the deamination of adenosine to inosine at the wobble position 34 of tRNA(Arg2).[HAMAP-Rule:MF_00972]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fluorescent probes provide an unparalleled opportunity to visualize and quantify dynamic events. Here, we employ a medium-size, cysteine specific coumarin based switch-ON fluorescent probe 'L' to track protein unfolding profiles and accessibility of cysteine residues in proteins. It was established that 'L' is highly selective and exhibits no artifact due to interaction with other bystander species. 'L' is able to gauge subtle changes in protein microenvironment and proved to be effective in delineating early unfolding events that are difficult to otherwise discern by classic techniques such as circular dichroism. By solving the X-ray structure of TadA and probing the temperature dependent fluorescence-ON response with native TadA and its cysteine mutants, it was revealed that unfolding occurs in a stage-wise manner and the regions that are functionally important form compact sub-domains and unfold at later stages. Our results assert that probe 'L' serves as an efficient tool to monitor subtle changes in protein structure and can be employed as a generic dye to study processes such as protein unfolding.

Deciphering protein microenvironment by using a cysteine specific switch-ON fluorescent probe.,Mariam J, Hoskere Ashoka A, Gaded V, Ali F, Malvi H, Das A, Anand R Org Biomol Chem. 2021 May 25. doi: 10.1039/d1ob00698c. PMID:34037063<ref>PMID:34037063</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7cph" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adenosine deaminase 3D structures|Adenosine deaminase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Large Structures]]
[[Category: Anand R]]
[[Category: Gaded V]]
[[Category: Mariam J]]