4pej

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:16, 27 September 2023) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 1: Line 1:
-
'''Unreleased structure'''
 
-
The entry 4pej is ON HOLD until Paper Publication
+
==Crystal structure of a computationally designed retro-aldolase, RA110.4 (Cys free)==
 +
<StructureSection load='4pej' size='340' side='right'caption='[[4pej]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[4pej]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PEJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PEJ 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]] 1.85&#8491;</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=4pej FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pej OCA], [https://pdbe.org/4pej PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4pej RCSB], [https://www.ebi.ac.uk/pdbsum/4pej PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4pej ProSAT]</span></td></tr>
 +
</table>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Enzyme-based tags attached to a protein-of-interest (POI) that react with a small molecule, rendering the conjugate fluorescent, are very useful for studying the POI in living cells. These tags are typically based on endogenous enzymes, so protein engineering is required to ensure that the small-molecule probe does not react with the endogenous enzyme in the cell of interest. Here we demonstrate that de novo-designed enzymes can be used as tags to attach to POIs. The inherent bioorthogonality of the de novo-designed enzyme-small-molecule probe reaction circumvents the need for protein engineering, since these enzyme activities are not present in living organisms. Herein, we transform a family of de novo-designed retroaldolases into variable-molecular-weight tags exhibiting fluorescence imaging, reporter, and electrophoresis applications that are regulated by tailored, reactive small-molecule fluorophores.
-
Authors: Bhabha, G., Zhang, X., Liu, Y., Ekiert, D.C.
+
De novo-designed enzymes as small-molecule-regulated fluorescence imaging tags and fluorescent reporters.,Liu Y, Zhang X, Tan YL, Bhabha G, Ekiert DC, Kipnis Y, Bjelic S, Baker D, Kelly JW J Am Chem Soc. 2014 Sep 24;136(38):13102-5. doi: 10.1021/ja5056356. Epub 2014 Sep, 11. PMID:25209927<ref>PMID:25209927</ref>
-
Description: Crystal structure of a computationally designed retro-aldolase, RA110.4 (Cys free)
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4pej" style="background-color:#fffaf0;"></div>
 +
 
 +
==See Also==
 +
*[[Aldolase 3D structures|Aldolase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Synthetic construct]]
 +
[[Category: Bhabha G]]
 +
[[Category: Ekiert DC]]
 +
[[Category: Liu Y]]
 +
[[Category: Zhang X]]

Current revision

Crystal structure of a computationally designed retro-aldolase, RA110.4 (Cys free)

PDB ID 4pej

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools