Proteopedia

1odn: Difference between revisions

← Older edit
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='1odn' size='340' side='right'caption='[[1odn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='1odn' size='340' side='right'caption='[[1odn]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1odn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/A._nidulans A. nidulans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODN FirstGlance]. <br>
<table><tr><td colspan='2'>[[1odn]] 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=1ODN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APV:6-(5-AMINO-5-CARBOXY-PENTANOYLAMINO)-3-HYDROXYMETHYL-7-OXO-4-THIA-1-AZA-BICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC+ACID'>APV</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bk0|1bk0]], [[1blz|1blz]], [[1hb1|1hb1]], [[1hb2|1hb2]], [[1hb3|1hb3]], [[1hb4|1hb4]], [[1ips|1ips]], [[1obn|1obn]], [[1odm|1odm]], [[1oc1|1oc1]], [[1qiq|1qiq]], [[1qje|1qje]], [[1qjf|1qjf]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APV:6-(5-AMINO-5-CARBOXY-PENTANOYLAMINO)-3-HYDROXYMETHYL-7-OXO-4-THIA-1-AZA-BICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC+ACID'>APV</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1odn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odn OCA], [https://pdbe.org/1odn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odn RCSB], [https://www.ebi.ac.uk/pdbsum/1odn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odn ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1odn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odn OCA], [https://pdbe.org/1odn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odn RCSB], [https://www.ebi.ac.uk/pdbsum/1odn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/IPNS_EMENI IPNS_EMENI]] Removes, in the presence of oxygen, 4 hydrogen atoms from delta-L-(alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV) to form the azetidinone and thiazolidine rings of isopenicillin.  
[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]]
Line 36: Line 36:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: A. nidulans]]
[[Category: Aspergillus nidulans]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Adlington, R M]]
[[Category: Adlington RM]]
[[Category: Baldwin, J E]]
[[Category: Baldwin JE]]
[[Category: Burzlaff, N I]]
[[Category: Burzlaff NI]]
[[Category: Clifton, I J]]
[[Category: Clifton IJ]]
[[Category: Elkins, J M]]
[[Category: Elkins JM]]
[[Category: Roach, P L]]
[[Category: Roach PL]]
[[Category: Rutledge, P J]]
[[Category: Rutledge PJ]]
[[Category: Antibiotic biosynthesis]]
[[Category: B-lactam antibiotic]]
[[Category: Oxidoreductase]]
[[Category: Oxygenase]]
[[Category: Penicillin biosynthesis]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/w/1odn"