5l7p

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'''Unreleased structure'''
 
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The entry 5l7p is ON HOLD until Paper Publication
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==In silico-powered specific incorporation of photocaged Dopa at multiple protein sites==
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<StructureSection load='5l7p' size='340' side='right' caption='[[5l7p]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5l7p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L7P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L7P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=BUU:(2~{S})-2-azanyl-3-[3-[(2-nitrophenyl)methoxy]-4-oxidanyl-phenyl]propanoic+acid'>BUU</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] </span></td></tr>
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<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=5l7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l7p OCA], [http://pdbe.org/5l7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l7p RCSB], [http://www.ebi.ac.uk/pdbsum/5l7p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l7p ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SYY_METJA SYY_METJA]] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).<ref>PMID:10585437</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Marine mussels exhibit potent underwater adhesion abilities under hostile conditions by employing 3,4-dihydroxyphenylalanine (DOPA)-rich mussel adhesive proteins (MAPs). However, their recombinant production is a major biotechnological challenge. Herein, a novel strategy based on genetic code expansion has been developed by engineering efficient aminoacyl-transfer RNA synthetases (aaRSs) for the photocaged noncanonical amino acid ortho-nitrobenzyl DOPA (ONB-DOPA). The engineered ONB-DOPARS enables in vivo production of MAP type 5 site-specifically equipped with multiple instances of ONB-DOPA to yield photocaged, spatiotemporally controlled underwater adhesives. Upon exposure to UV light, these proteins feature elevated wet adhesion properties. This concept offers new perspectives for the production of recombinant bioadhesives.
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Authors:
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Photoactivatable Mussel-Based Underwater Adhesive Proteins by an Expanded Genetic Code.,Hauf M, Richter F, Schneider T, Faidt T, Martins BM, Baumann T, Durkin P, Dobbek H, Jacobs K, Moglich A, Budisa N Chembiochem. 2017 Jun 26. doi: 10.1002/cbic.201700327. PMID:28650092<ref>PMID:28650092</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5l7p" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Tyrosine--tRNA ligase]]
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[[Category: Baumann, T]]
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[[Category: Budisa, N]]
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[[Category: Dobbek, H]]
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[[Category: Durkin, P]]
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[[Category: Hauf, M]]
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[[Category: Martins, B M]]
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[[Category: Moeglich, A]]
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[[Category: Richter, F]]
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[[Category: Schneider, T]]
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[[Category: Ligase]]
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[[Category: Tyrr]]

Revision as of 10:44, 13 September 2017

In silico-powered specific incorporation of photocaged Dopa at multiple protein sites

5l7p, resolution 1.90Å

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