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2vbp

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==ISOPENICILLIN N SYNTHASE WITH SUBSTRATE ANALOGUE L,L,L-ACAB (UNEXPOSED)==
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<StructureSection load='2vbp' size='340' side='right' caption='[[2vbp]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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==Isopenicillin N synthase with substrate analogue L,L,L-ACAB (unexposed)==
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<StructureSection load='2vbp' size='340' side='right'caption='[[2vbp]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2vbp]] is a 1 chain structure with 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=2VBP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VBP FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2vbp]] 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=2VBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VBP FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VB1:N^6^-[(1R)-2-{[(1S)-1-CARBOXYPROPYL]AMINO}-2-OXO-1-(SULFANYLMETHYL)ETHYL]-6-OXO-L-LYSINE'>VB1</scene><br>
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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]] 1.5&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bk0|1bk0]], [[1blz|1blz]], [[1hb2|1hb2]], [[1hb3|1hb3]], [[1hb4|1hb4]], [[1obn|1obn]], [[1odm|1odm]], [[1odn|1odn]], [[1qiq|1qiq]], [[1qje|1qje]], [[1qjf|1qjf]], [[1uzw|1uzw]], [[1w03|1w03]], [[1w06|1w06]], [[1w3x|1w3x]], [[2bu9|2bu9]], [[2ivi|2ivi]], [[2ivj|2ivj]], [[2vbb|2vbb]], [[1hb1|1hb1]], [[1ips|1ips]], [[1oc1|1oc1]], [[1w04|1w04]], [[1w05|1w05]], [[1w3v|1w3v]], [[2bjs|2bjs]], [[2jb4|2jb4]], [[2vau|2vau]], [[2vbd|2vbd]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VB1:N^6^-[(1R)-2-{[(1S)-1-CARBOXYPROPYL]AMINO}-2-OXO-1-(SULFANYLMETHYL)ETHYL]-6-OXO-L-LYSINE'>VB1</scene></td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isopenicillin-N_synthase Isopenicillin-N synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.21.3.1 1.21.3.1] </span></td></tr>
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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=2vbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vbp OCA], [https://pdbe.org/2vbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vbp RCSB], [https://www.ebi.ac.uk/pdbsum/2vbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vbp ProSAT]</span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vbp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vbp RCSB], [http://www.ebi.ac.uk/pdbsum/2vbp PDBsum]</span></td></tr>
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</table>
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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: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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vb/2vbp_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vb/2vbp_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2vbp ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 2vbp" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Emericella nidulans]]
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[[Category: Aspergillus nidulans]]
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[[Category: Isopenicillin-N synthase]]
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[[Category: Large Structures]]
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[[Category: Adlington, R M.]]
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[[Category: Adlington RM]]
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[[Category: Baldwin, J E.]]
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[[Category: Baldwin JE]]
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[[Category: Clifton, I J.]]
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[[Category: Clifton IJ]]
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[[Category: Ge, W.]]
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[[Category: Ge W]]
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[[Category: Rutledge, P J.]]
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[[Category: Rutledge PJ]]
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[[Category: Antibiotic biosynthesis]]
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[[Category: B-lactam antibiotic]]
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[[Category: Iron]]
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[[Category: Metal-binding]]
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[[Category: Monocyclic intermediate]]
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[[Category: Oxidoreductase]]
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[[Category: Oxygenase]]
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[[Category: Penicillin biosynthesis]]
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[[Category: Vitamin c]]
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Current revision

Isopenicillin N synthase with substrate analogue L,L,L-ACAB (unexposed)

PDB ID 2vbp

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