View source for 4tvw


==Resorufin ligase with bound resorufin-AMP analog==
<StructureSection load='4tvw' size='340' side='right'caption='[[4tvw]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4tvw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TVW 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]] 3.505&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=37P:5-O-{[5-(7-HYDROXY-3-OXO-3H-PHENOXAZIN-2-YL)PENTANOYL]SULFAMOYL}ADENOSINE'>37P</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=4tvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tvw OCA], [https://pdbe.org/4tvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tvw RCSB], [https://www.ebi.ac.uk/pdbsum/4tvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tvw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LPLA_ECOLI LPLA_ECOLI] Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein.<ref>PMID:7639702</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Chemical fluorophores offer tremendous size and photophysical advantages over fluorescent proteins but are much more challenging to target to specific cellular proteins. Here, we used Rosetta-based computation to design a fluorophore ligase that accepts the red dye resorufin, starting from Escherichia coli lipoic acid ligase. X-ray crystallography showed that the design closely matched the experimental structure. Resorufin ligase catalyzed the site-specific and covalent attachment of resorufin to various cellular proteins genetically fused to a 13-aa recognition peptide in multiple mammalian cell lines and in primary cultured neurons. We used resorufin ligase to perform superresolution imaging of the intermediate filament protein vimentin by stimulated emission depletion and electron microscopies. This work illustrates the power of Rosetta for major redesign of enzyme specificity and introduces a tool for minimally invasive, highly specific imaging of cellular proteins by both conventional and superresolution microscopies.

Computational design of a red fluorophore ligase for site-specific protein labeling in living cells.,Liu DS, Nivon LG, Richter F, Goldman PJ, Deerinck TJ, Yao JZ, Richardson D, Phipps WS, Ye AZ, Ellisman MH, Drennan CL, Baker D, Ting AY Proc Natl Acad Sci U S A. 2014 Oct 13. pii: 201404736. PMID:25313043<ref>PMID:25313043</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4tvw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Drennan CL]]
[[Category: Goldman PJ]]