8py5

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m (Protected "8py5" [edit=sysop:move=sysop])
Current revision (05:38, 7 August 2024) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 8py5 is ON HOLD until Paper Publication
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==Isopenicillin N synthase in complex with Fe and ACdV under anaerobic conditions==
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<StructureSection load='8py5' size='340' side='right'caption='[[8py5]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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Authors: Rabe, P., Schofield, C.J.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8py5]] 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=8PY5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PY5 FirstGlance]. <br>
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Description: Isopenicillin N synthase in complex with Fe and ACdV under anaerobic conditions
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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]] 1.85&#8491;</td></tr>
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[[Category: Unreleased Structures]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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[[Category: Rabe, P]]
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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=8py5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8py5 OCA], [https://pdbe.org/8py5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8py5 RCSB], [https://www.ebi.ac.uk/pdbsum/8py5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8py5 ProSAT]</span></td></tr>
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[[Category: Schofield, C.J]]
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</table>
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== Function ==
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[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:11755401, PubMed:3319778). 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:11755401, PubMed:28703303, PubMed:3319778). 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>
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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: Aspergillus nidulans FGSC A4]]
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[[Category: Large Structures]]
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[[Category: Rabe P]]
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[[Category: Schofield CJ]]

Current revision

Isopenicillin N synthase in complex with Fe and ACdV under anaerobic conditions

PDB ID 8py5

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