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2ivj

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(New page: 200px<br /> <applet load="2ivj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ivj, resolution 1.46&Aring;" /> '''ISOPENICILLIN N SYN...)
Current revision (09:30, 9 May 2024) (edit) (undo)
 
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[[Image:2ivj.gif|left|200px]]<br />
 
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<applet load="2ivj" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2ivj, resolution 1.46&Aring;" />
 
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'''ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (ANAEROBIC AC-CYCLOPROPYLGLYCINE FE COMPLEX)'''<br />
 
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==About this Structure==
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==Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac- cyclopropylglycine Fe Complex)==
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2IVJ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Emericella_nidulans Emericella nidulans]] with SO4, FE2 and BCV as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IVJ OCA]].
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<StructureSection load='2ivj' size='340' side='right'caption='[[2ivj]], [[Resolution|resolution]] 1.46&Aring;' scene=''>
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[[Category: Emericella nidulans]]
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== Structural highlights ==
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[[Category: Single protein]]
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<table><tr><td colspan='2'>[[2ivj]] is a 1 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=2IVJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IVJ FirstGlance]. <br>
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[[Category: Adlington, R.M.]]
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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]] 1.46&#8491;</td></tr>
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[[Category: Baldwin, J.E.]]
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCV:D-(L-A-AMINOADIPOYL)-L-CYSTEINYL-D-CYCLOPROPYLGLYCINE'>BCV</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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[[Category: Clifton, I.J.]]
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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=2ivj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ivj OCA], [https://pdbe.org/2ivj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ivj RCSB], [https://www.ebi.ac.uk/pdbsum/2ivj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ivj ProSAT]</span></td></tr>
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[[Category: Elkins, J.M.]]
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</table>
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[[Category: Howard-Jones, A.R.]]
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== Function ==
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[[Category: Roach, P.L.]]
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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: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>
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[[Category: Rutledge, P.J.]]
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== Evolutionary Conservation ==
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[[Category: BCV]]
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[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: FE2]]
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Check<jmol>
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[[Category: SO4]]
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<jmolCheckbox>
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[[Category: antbiotic biosynthesis]]
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/iv/2ivj_consurf.spt"</scriptWhenChecked>
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[[Category: antibiotic biosynthesis]]
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: b-lactam antibiotic]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: iron]]
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</jmolCheckbox>
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[[Category: metal-binding]]
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</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=2ivj ConSurf].
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[[Category: oxidoreductase]]
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<div style="clear:both"></div>
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[[Category: oxygenase]]
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<div style="background-color:#fffaf0;">
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[[Category: penicillin biosynthesis]]
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== Publication Abstract from PubMed ==
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[[Category: vitamin c]]
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Isopenicillin N synthase (IPNS), a non-heme iron oxidase central to penicillin and cephalosporin biosynthesis, catalyzes an energetically demanding chemical transformation to produce isopenicillin N from the tripeptide delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-valine (ACV). We describe the synthesis of two cyclopropyl-containing tripeptide analogues, delta-(l-alpha-aminoadipoyl)-l-cysteinyl-beta-methyl-d-cyclopropylglycine and delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-cyclopropylglycine, designed as probes for the mechanism of IPNS. We have solved the X-ray crystal structures of these substrates in complex with IPNS and propose a revised mechanism for the IPNS-mediated turnover of these compounds. Relative to the previously determined IPNS-Fe(II)-ACV structure, key differences exist in substrate orientation and water occupancy, which allow for an explanation of the differences in reactivity of these substrates.
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:53:09 2007''
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Interactions of isopenicillin N synthase with cyclopropyl-containing substrate analogues reveal new mechanistic insight.,Howard-Jones AR, Elkins JM, Clifton IJ, Roach PL, Adlington RM, Baldwin JE, Rutledge PJ Biochemistry. 2007 Apr 24;46(16):4755-62. Epub 2007 Mar 31. PMID:17397141<ref>PMID:17397141</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ivj" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Isopenicillin N synthase|Isopenicillin N synthase]]
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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]]
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[[Category: Large Structures]]
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[[Category: Adlington RM]]
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[[Category: Baldwin JE]]
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[[Category: Clifton IJ]]
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[[Category: Elkins JM]]
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[[Category: Howard-Jones AR]]
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[[Category: Roach PL]]
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[[Category: Rutledge PJ]]

Current revision

Isopenicillin N Synthase From Aspergillus Nidulans (Anaerobic Ac- cyclopropylglycine Fe Complex)

PDB ID 2ivj

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