4cs2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "4cs2" [edit=sysop:move=sysop])
Line 1: Line 1:
-
'''Unreleased structure'''
+
==Catalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in its apo form==
 +
<StructureSection load='4cs2' size='340' side='right' caption='[[4cs2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 +
== Structural highlights ==
 +
[[4cs2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CS2 OCA]. <br>
 +
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
 +
== Publication Abstract from PubMed ==
 +
The site-selective introduction of photo-crosslinking groups into proteins enables the discovery and mapping of weak and/or transient protein interactions with high spatiotemporal resolution, both in vitro and in vivo. We report the genetic encoding of a furan-based, photo-crosslinking amino acid in human cells; it can be activated with red light, thus offering high penetration depths in biological samples. This is achieved by activation of the amino acid and charging to its cognate tRNA by a pyrrolysyl-tRNA-synthetase (PylRS) mutant with broad polyspecificity. To gain insights into the recognition of this amino acid and to provide a rationale for its polyspecificity, we solved three crystal structures of the PylRS mutant: in its apo-form, in complex with adenosine 5'-(beta,gamma-imido)triphosphate (AMP-PNP) and in complex with the AMP ester of the furan amino acid. These structures provide clues for the observed polyspecificity and represent a promising starting point for the engineering of PylRS mutants with further increased substrate scope.
-
The entry 4cs2 is ON HOLD until Paper Publication
+
Structural Basis of Furan-Amino Acid Recognition by a Polyspecific Aminoacyl-tRNA-Synthetase and its Genetic Encoding in Human Cells.,Schmidt MJ, Weber A, Pott M, Welte W, Summerer D Chembiochem. 2014 Apr 15. doi: 10.1002/cbic.201402006. PMID:24737732<ref>PMID:24737732</ref>
-
Authors: Schmidt, M.J., Weber, A., Pott, M., Welte, W., Summerer, D.
+
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-
 
+
== References ==
-
Description: Catalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in its apo form
+
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Pott, M.]]
 +
[[Category: Schmidt, M J.]]
 +
[[Category: Summerer, D.]]
 +
[[Category: Weber, A.]]
 +
[[Category: Welte, W.]]
 +
[[Category: Ligase]]

Revision as of 07:52, 30 April 2014

Catalytic domain of Pyrrolysyl-tRNA synthetase mutant Y306A, Y384F in its apo form

4cs2, resolution 1.90Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools