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5tu6

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Current revision (14:23, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5tu6' size='340' side='right'caption='[[5tu6]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
<StructureSection load='5tu6' size='340' side='right'caption='[[5tu6]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tu6]] is a 2 chain structure with sequence from [http://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=5TU6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TU6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tu6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Planktothrix_agardhii_NIES-596 Planktothrix agardhii NIES-596] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TU6 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=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</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]] 2.22&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tty|5tty]], [[5tu4|5tu4]], [[5tu5|5tu5]]</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=DST:DIMETHYLALLYL+S-THIOLODIPHOSPHATE'>DST</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pagF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=443922 Planktothrix agardhii NIES-596])</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=5tu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tu6 OCA], [https://pdbe.org/5tu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tu6 RCSB], [https://www.ebi.ac.uk/pdbsum/5tu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tu6 ProSAT]</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=5tu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tu6 OCA], [http://pdbe.org/5tu6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tu6 RCSB], [http://www.ebi.ac.uk/pdbsum/5tu6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tu6 ProSAT]</span></td></tr>
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</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 5tu6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Planktothrix agardhii nies-596]]
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[[Category: Planktothrix agardhii NIES-596]]
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[[Category: Hao, Y]]
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[[Category: Synthetic construct]]
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[[Category: Nair, S K]]
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[[Category: Hao Y]]
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[[Category: Abba fold]]
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[[Category: Nair SK]]
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[[Category: Prenylation]]
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[[Category: Ripp]]
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[[Category: Transferase]]
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Current revision

PagF prenyltransferase with cyclic[INPYLYP] and DMSPP

PDB ID 5tu6

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