4s02
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Biphenylalanine modified threonyl-tRNA synthetase from Pyrococcus abyssi: I11BIF, F42W, Y79A, and F123Y mutant== |
+ | <StructureSection load='4s02' size='340' side='right' caption='[[4s02]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4s02]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S02 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | ||
+ | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BIF:(R)-2-AMINO-3-(4-PHENYLCYCLOHEXYL)PROPANOIC+ACID'>BIF</scene></td></tr> | ||
+ | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y2q|1y2q]]</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </span></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4s02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4s02 RCSB], [http://www.ebi.ac.uk/pdbsum/4s02 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The fleeting lifetimes of the transition states (TSs) of chemical reactions make determination of their three-dimensional structures by diffraction methods a challenge. Here, we used packing interactions within the core of a protein to stabilize the planar TS conformation for rotation around the central carbon-carbon bond of biphenyl so that it could be directly observed by x-ray crystallography. The computational protein design software Rosetta was used to design a pocket within threonyl-transfer RNA synthetase from the thermophile Pyrococcus abyssi that forms complementary van der Waals interactions with a planar biphenyl. This latter moiety was introduced biosynthetically as the side chain of the noncanonical amino acid p-biphenylalanine. Through iterative rounds of computational design and structural analysis, we identified a protein in which the side chain of p-biphenylalanine is trapped in the energetically disfavored, coplanar conformation of the TS of the bond rotation reaction. | ||
- | + | Transition states. Trapping a transition state in a computationally designed protein bottle.,Pearson AD, Mills JH, Song Y, Nasertorabi F, Han GW, Baker D, Stevens RC, Schultz PG Science. 2015 Feb 20;347(6224):863-7. doi: 10.1126/science.aaa2424. PMID:25700516<ref>PMID:25700516</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
+ | </StructureSection> | ||
+ | [[Category: Threonine--tRNA ligase]] | ||
+ | [[Category: Baker, D]] | ||
+ | [[Category: Han, G W]] | ||
+ | [[Category: Mills, J H]] | ||
[[Category: Nasertorabi, F]] | [[Category: Nasertorabi, F]] | ||
+ | [[Category: Pearson, A D]] | ||
+ | [[Category: Schultz, P G]] | ||
[[Category: Song, Y]] | [[Category: Song, Y]] | ||
- | [[Category: Stevens, R | + | [[Category: Stevens, R C]] |
- | [[Category: | + | [[Category: Beta-alpha-beta fold]] |
- | [[Category: | + | [[Category: Biphenylalanine and unnatural amino acid]] |
- | [[Category: | + | [[Category: Editing domain]] |
- | [[Category: | + | [[Category: Ligase]] |
+ | [[Category: Threonine-trna ligase]] | ||
+ | [[Category: Trna-synthetase]] |
Revision as of 12:03, 18 March 2015
Biphenylalanine modified threonyl-tRNA synthetase from Pyrococcus abyssi: I11BIF, F42W, Y79A, and F123Y mutant
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