5tu4

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==PagF with Boc-Tyr and DMSPP==
==PagF with Boc-Tyr and DMSPP==
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<StructureSection load='5tu4' size='340' side='right' caption='[[5tu4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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<StructureSection load='5tu4' size='340' side='right'caption='[[5tu4]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tu4]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TU4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TU4 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tu4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Planktothrix_agardhii_NIES-596 Planktothrix agardhii NIES-596]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TU4 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=B1C:N-(TERT-BUTOXYCARBONYL)-L-TYROSINE'>B1C</scene>, <scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tyy|5tyy]], [[5tu5|5tu5]], [[5tu6|5tu6]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1C:N-(TERT-BUTOXYCARBONYL)-L-TYROSINE'>B1C</scene>, <scene name='pdbligand=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=5tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tu4 OCA], [http://pdbe.org/5tu4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tu4 RCSB], [http://www.ebi.ac.uk/pdbsum/5tu4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tu4 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5tu4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tu4 OCA], [https://pdbe.org/5tu4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tu4 RCSB], [https://www.ebi.ac.uk/pdbsum/5tu4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tu4 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/F5B6Z0_PLAAG F5B6Z0_PLAAG]
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The cyanobactin prenyltransferases catalyze a series of known or unprecedented reactions on millions of different substrates, with no easily observable recognition motif and exquisite regioselectivity. Here we define the basis of broad substrate tolerance for the otherwise uncharacterized TruF family. We determined the structures of the Tyr-prenylating enzyme PagF, in complex with an isoprenoid donor analog and a panel of linear and macrocyclic peptide substrates. Unexpectedly, the structures reveal a truncated barrel fold, wherein binding of large peptide substrates is necessary to complete a solvent-exposed hydrophobic pocket to form the catalytically competent active site. Kinetic, mutational, chemical, and computational analyses revealed the structural basis of selectivity, showing a small motif within peptide substrates that is sufficient for recognition by the enzyme. Attaching this 2-residue motif to two random peptides results in their isoprenylation by PagF, demonstrating utility as a general biocatalytic platform for modifications on any peptide substrate.
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Molecular basis for the broad substrate selectivity of a peptide prenyltransferase.,Hao Y, Pierce E, Roe D, Morita M, McIntosh JA, Agarwal V, Cheatham TE 3rd, Schmidt EW, Nair SK Proc Natl Acad Sci U S A. 2016 Dec 6;113(49):14037-14042. Epub 2016 Nov 21. PMID:27872314<ref>PMID:27872314</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5tu4" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Hao, Y]]
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[[Category: Large Structures]]
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[[Category: Nair, S K]]
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[[Category: Planktothrix agardhii NIES-596]]
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[[Category: Abba fold]]
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[[Category: Hao Y]]
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[[Category: Prenylation]]
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[[Category: Nair SK]]
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[[Category: Ripp]]
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[[Category: Transferase]]
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Current revision

PagF with Boc-Tyr and DMSPP

PDB ID 5tu4

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