7poy: Difference between revisions

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<StructureSection load='7poy' size='340' side='right'caption='[[7poy]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='7poy' size='340' side='right'caption='[[7poy]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7poy]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7POY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7POY FirstGlance]. <br>
<table><tr><td colspan='2'>[[7poy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans_FGSC_A4 Aspergillus nidulans FGSC A4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7POY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7POY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=81T:~{N}-[(3~{R})-2,2,5,5-tetramethyl-1-oxidanyl-pyrrolidin-3-yl]ethanamide'>81T</scene>, <scene name='pdbligand=ACV:L-D-(A-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE'>ACV</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</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" id="ligandDat"><scene name='pdbligand=81T:~{N}-[(3~{R})-2,2,5,5-tetramethyl-1-oxidanyl-pyrrolidin-3-yl]ethanamide'>81T</scene>, <scene name='pdbligand=ACV:L-D-(A-AMINOADIPOYL)-L-CYSTEINYL-D-VALINE'>ACV</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=NO:NITRIC+OXIDE'>NO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6zam|6zam]], [[6zap|6zap]], [[6zan|6zan]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Isopenicillin-N_synthase Isopenicillin-N synthase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7poy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7poy OCA], [https://pdbe.org/7poy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7poy RCSB], [https://www.ebi.ac.uk/pdbsum/7poy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7poy ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7poy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7poy OCA], [https://pdbe.org/7poy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7poy RCSB], [https://www.ebi.ac.uk/pdbsum/7poy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7poy ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/IPNS_EMENI IPNS_EMENI]] Removes, in the presence of oxygen, 4 hydrogen atoms from delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to form the azetidinone and thiazolidine rings of isopenicillin.  
[[https://www.uniprot.org/uniprot/IPNA_EMENI IPNA_EMENI]] Isopenicillin N synthase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:3319778, PubMed:11755401). IpnA catalyzes the cyclization of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) to form isopenicillin N (IPN) that contains the beta-lactam nucleus (PubMed:3319778, PubMed:11755401, PubMed:28703303). The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase penDE to yield penicillin in the peroxisomal matrix (By similarity).[UniProtKB:P08703]<ref>PMID:11755401</ref> <ref>PMID:28703303</ref> <ref>PMID:3319778</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Isopenicillin-N synthase]]
[[Category: Aspergillus nidulans FGSC A4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Clifton, I]]
[[Category: Clifton I]]
[[Category: Rabe, P]]
[[Category: Rabe P]]
[[Category: Schofield, C J]]
[[Category: Schofield CJ]]
[[Category: Walla, C]]
[[Category: Walla C]]
[[Category: Isopenicillin n synthase]]
[[Category: Oxidase]]
[[Category: Oxidoreductase]]
[[Category: Penicillin biosynthesis]]
[[Category: Spin labeled protein]]
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