5n82
From Proteopedia
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<StructureSection load='5n82' size='340' side='right' caption='[[5n82]], [[Resolution|resolution]] 1.71Å' scene=''> | <StructureSection load='5n82' size='340' side='right' caption='[[5n82]], [[Resolution|resolution]] 1.71Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5n82]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N82 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5n82]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_10027 Atcc 10027]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5N82 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5N82 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8PZ:[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+~{N}-[(3~{S})-3-azanyl-3-phenyl-propanoyl]sulfamate'>8PZ</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=8PZ:[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methyl+~{N}-[(3~{S})-3-azanyl-3-phenyl-propanoyl]sulfamate'>8PZ</scene>, <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tycA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=54914 ATCC 10027])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylalanine_racemase_(ATP-hydrolyzing) Phenylalanine racemase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.11 5.1.1.11] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phenylalanine_racemase_(ATP-hydrolyzing) Phenylalanine racemase (ATP-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.1.1.11 5.1.1.11] </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=5n82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n82 OCA], [http://pdbe.org/5n82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n82 RCSB], [http://www.ebi.ac.uk/pdbsum/5n82 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n82 ProSAT]</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=5n82 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5n82 OCA], [http://pdbe.org/5n82 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5n82 RCSB], [http://www.ebi.ac.uk/pdbsum/5n82 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5n82 ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/TYCA_BREPA TYCA_BREPA]] In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer. | [[http://www.uniprot.org/uniprot/TYCA_BREPA TYCA_BREPA]] In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Biosynthetic modification of nonribosomal peptide backbones represents a potentially powerful strategy to modulate the structure and properties of an important class of therapeutics. Using a high-throughput assay for catalytic activity, we show here that an L-Phe-specific module of an archetypal nonribosomal peptide synthetase can be reprogrammed to accept and process the backbone-modified amino acid (S)-beta-Phe with near-native specificity and efficiency. A co-crystal structure with a non-hydrolysable aminoacyl-AMP analogue reveals the origins of the 40,000-fold alpha/beta-specificity switch, illuminating subtle but precise remodelling of the active site. When the engineered catalyst was paired with downstream module(s), (S)-beta-Phe-containing peptides were produced at preparative scale in vitro (~1 mmol) and high titres in vivo (~100 mg l(-1)), highlighting the potential of biosynthetic pathway engineering for the construction of novel nonribosomal beta-frameworks. | ||
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| + | Nonribosomal biosynthesis of backbone-modified peptides.,Niquille DL, Hansen DA, Mori T, Fercher D, Kries H, Hilvert D Nat Chem. 2018 Mar;10(3):282-287. doi: 10.1038/nchem.2891. Epub 2017 Nov 20. PMID:29461527<ref>PMID:29461527</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5n82" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 10027]] | ||
[[Category: Fercher, D]] | [[Category: Fercher, D]] | ||
[[Category: Hansen, D L]] | [[Category: Hansen, D L]] | ||
Revision as of 07:07, 28 February 2018
Crystal structure of an engineered TycA variant in complex with an beta-Phe-AMP analog
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