9hwf: Difference between revisions

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'''Unreleased structure'''


The entry 9hwf is ON HOLD  until Paper Publication
==Isopenicillin N synthase N252E variant in complex with Fe and IPN after O2 exposure==
 
<StructureSection load='9hwf' size='340' side='right'caption='[[9hwf]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
Authors: Rabe, P., Schofield, C.J., Stead, A.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[9hwf]] 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=9HWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9HWF FirstGlance]. <br>
Description: Isopenicillin N synthase N252E variant in complex with Fe and IPN after O2 expsure
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
[[Category: Unreleased Structures]]
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=IP1:ISOPENICILLIN+N'>IP1</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
[[Category: Stead, A]]
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9hwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9hwf OCA], [https://pdbe.org/9hwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9hwf RCSB], [https://www.ebi.ac.uk/pdbsum/9hwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9hwf ProSAT]</span></td></tr>
[[Category: Schofield, C.J]]
</table>
[[Category: Rabe, P]]
== Function ==
[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>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aspergillus nidulans FGSC A4]]
[[Category: Large Structures]]
[[Category: Rabe P]]
[[Category: Schofield CJ]]
[[Category: Stead A]]

Latest revision as of 08:49, 14 January 2026

Isopenicillin N synthase N252E variant in complex with Fe and IPN after O2 exposure

9hwf, resolution 1.40Å

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