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[[Image:1ips.jpg|left|200px]]


{{Structure
==ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)==
|PDB= 1ips |SIZE=350|CAPTION= <scene name='initialview01'>1ips</scene>, resolution 2.5&Aring;
<StructureSection load='1ips' size='340' side='right'caption='[[1ips]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
|SITE= <scene name='pdbsite=SA:Active+Site+(Mn+Binding),+A+Chain'>SA</scene> and <scene name='pdbsite=SB:Active+Site+(Mn+Binding),+B+Chain'>SB</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
<table><tr><td colspan='2'>[[1ips]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_nidulans Aspergillus nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IPS FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
|GENE= PCB C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=162425 Emericella nidulans])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ips FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ips OCA], [https://pdbe.org/1ips PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ips RCSB], [https://www.ebi.ac.uk/pdbsum/1ips PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ips ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ips FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ips OCA], [http://www.ebi.ac.uk/pdbsum/1ips PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ips RCSB]</span>
== 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: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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ip/1ips_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ips ConSurf].
<div style="clear:both"></div>


'''ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)'''
==See Also==
 
*[[Isopenicillin N synthase|Isopenicillin N synthase]]
 
== References ==
==Overview==
<references/>
Penicillin antibiotics are all produced from fermentation-derived penicillins because their chemical synthesis is not commercially viable. The key step in penicillin biosynthesis, in which both the beta-lactam and thiazolidine rings of the nucleus are created, is mediated by isopenicillin N synthase (IPNS), which binds ferrous iron and uses dioxygen as a cosubstrate. In a unique enzymatic step, with no chemical precedent, IPNS catalyses the transfer of four hydrogen atoms from its tripeptide substrate to dioxygen forming, in a single reaction, the complete bicyclic nucleus of the penicillins. We now report the structure of IPNS complexed with manganese, which reveals the active site is unusually buried within a 'jelly-roll' motif and lined by hydrophobic residues, and suggest how this structure permits the process of penicillin formation. Sequence analyses indicate IPNS, 1-aminocyclopropane-1-carboxylic acid oxidase and many of the 2-oxo-acid-dependent oxygenases contain a conserved jelly-roll motif, forming a new structural family of enzymes.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Aspergillus nidulans]]
1IPS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IPS OCA].
[[Category: Large Structures]]
 
[[Category: Andersson I]]
==Reference==
[[Category: Baldwin JE]]
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes., Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE, Nature. 1995 Jun 22;375(6533):700-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7791906 7791906]
[[Category: Barton GJ]]
[[Category: Emericella nidulans]]
[[Category: Clifton IJ]]
[[Category: Single protein]]
[[Category: Fulop V]]
[[Category: Andersson, I.]]
[[Category: Hajdu J]]
[[Category: Baldwin, J E.]]
[[Category: Harlos K]]
[[Category: Barton, G J.]]
[[Category: Roach PL]]
[[Category: Clifton, I J.]]
[[Category: Schofield CJ]]
[[Category: Fulop, V.]]
[[Category: Hajdu, J.]]
[[Category: Harlos, K.]]
[[Category: Roach, P L.]]
[[Category: Schofield, C J.]]
[[Category: antibiotic biosynthesis]]
[[Category: b-lactam antibiotic]]
[[Category: oxidoreductase]]
[[Category: oxygenase]]
[[Category: penicillin biosynthesis]]
 
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