2vau

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{{Seed}}
 
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[[Image:2vau.png|left|200px]]
 
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==Isopenicillin N synthase with substrate analogue ACOMP (unexposed)==
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The line below this paragraph, containing "STRUCTURE_2vau", creates the "Structure Box" on the page.
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<StructureSection load='2vau' size='340' side='right'caption='[[2vau]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2vau]] 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=2VAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VAU FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.8&#8491;</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=V20:N6^-[(1R)-2-[(1S)-1-CARBOXY-2-(METHYLSULFANYL)ETHOXY]-2-OXO-1-(SULFANYLMETHYL)ETHYL]-6-OXO-L-LYSINE'>V20</scene></td></tr>
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{{STRUCTURE_2vau| PDB=2vau | SCENE= }}
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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=2vau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vau OCA], [https://pdbe.org/2vau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vau RCSB], [https://www.ebi.ac.uk/pdbsum/2vau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vau ProSAT]</span></td></tr>
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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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/va/2vau_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</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/main_output.php?pdb_ID=2vau ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Isopenicillin N synthase (IPNS) is a nonheme iron oxidase that catalyzes the central step in the biosynthesis of beta-lactam antibiotics: oxidative cyclization of the linear tripeptide delta- l-alpha-aminoadipoyl- l-cysteinyl- d-valine (ACV) to isopenicillin N (IPN). The ACV analogue delta- l-alpha-aminoadipoyl- l-cysteine (1-( S)-carboxy-2-thiomethyl)ethyl ester (AC OmC) has been synthesized as a mechanistic probe of IPNS catalysis and crystallized with the enzyme. The crystal structure of the anaerobic IPNS/Fe(II)/AC OmC complex was determined to 1.80 A resolution, revealing a highly congested active site region. By exposing these anaerobically grown crystals to high-pressure oxygen gas, an unexpected sulfenate product has been observed, complexed to iron within the IPNS active site. A mechanism is proposed for formation of the sulfenate-iron complex, and it appears that AC OmC follows a different reaction pathway at the earliest stages of its reaction with IPNS. Thus it seems that oxygen (the cosubstrate) binds in a different site to that observed in previous studies with IPNS, displacing a water ligand from iron in the process. The iron-mediated conversion of metal-bound thiolate to sulfenate has not previously been observed in crystallographic studies with IPNS. This mode of reactivity is of particular interest when considered in the context of another family of nonheme iron enzymes, the nitrile hydratases, in which post-translational oxidation of two cysteine thiolates to sulfenic and sulfinic acids is essential for enzyme activity.
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===ISOPENICILLIN N SYNTHASE WITH SUBSTRATE ANALOGUE ACOMP (UNEXPOSED)===
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Isopenicillin N Synthase Mediates Thiolate Oxidation to Sulfenate in a Depsipeptide Substrate Analogue: Implications for Oxygen Binding and a Link to Nitrile Hydratase?,Ge W, Clifton IJ, Stok JE, Adlington RM, Baldwin JE, Rutledge PJ J Am Chem Soc. 2008 Jul 12. PMID:18620394<ref>PMID:18620394</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 2vau" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18620394}}, adds the Publication Abstract to the page
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*[[Isopenicillin N synthase|Isopenicillin N synthase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18620394 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18620394}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Aspergillus nidulans]]
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2VAU is a 1 chain 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=2VAU OCA].
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[[Category: Large Structures]]
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[[Category: Adlington RM]]
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==Reference==
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[[Category: Baldwin JE]]
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<ref group="xtra">PMID:18620394</ref><references group="xtra"/>
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[[Category: Clifton IJ]]
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[[Category: Emericella nidulans]]
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[[Category: Ge W]]
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[[Category: Isopenicillin-N synthase]]
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[[Category: Rutledge PJ]]
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[[Category: Adlington, R M.]]
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[[Category: Baldwin, J E.]]
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[[Category: Clifton, I J.]]
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[[Category: Ge, W.]]
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[[Category: Rutledge, P J.]]
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:06:20 2009''
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Current revision

Isopenicillin N synthase with substrate analogue ACOMP (unexposed)

PDB ID 2vau

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