1w3v
From Proteopedia
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|PDB= 1w3v |SIZE=350|CAPTION= <scene name='initialview01'>1w3v</scene>, resolution 1.40Å | |PDB= 1w3v |SIZE=350|CAPTION= <scene name='initialview01'>1w3v</scene>, resolution 1.40Å | ||
|SITE= <scene name='pdbsite=AC1:Mdz+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Mdz+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> | + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=MDZ:N~6~-METHYL-6-OXO-L-LYSINE+-+2-[(3-MERCAPTOBUTANOYL)OXY]-3-METHYLBUTANOIC+ACID'>MDZ</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <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> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1w3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w3v OCA], [http://www.ebi.ac.uk/pdbsum/1w3v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w3v RCSB]</span> | ||
}} | }} | ||
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[[Category: Daruzzaman, A.]] | [[Category: Daruzzaman, A.]] | ||
[[Category: Rutledge, P J.]] | [[Category: Rutledge, P J.]] | ||
| - | [[Category: FE2]] | ||
| - | [[Category: MDZ]] | ||
[[Category: 3d-structure]] | [[Category: 3d-structure]] | ||
[[Category: antibiotic biosynthesis]] | [[Category: antibiotic biosynthesis]] | ||
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[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:30:51 2008'' |
Revision as of 21:30, 30 March 2008
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| , resolution 1.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Isopenicillin-N synthase, with EC number 1.21.3.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ISOPENICILLIN N SYNTHASE D-(L-A-AMINOADIPOYL)-(3R)-METHYL-L-CYSTEINE D-A-HYDROXYISOVALERYL ESTER COMPLEX (ANAEROBIC)
Overview
Isopenicillin N synthase (IPNS) is a non-heme iron(ii)-dependent oxidase that is central to penicillin biosynthesis. Herein, we report mechanistic studies of the IPNS reaction in the crystalline state, using the substrate analogue delta-(L-alpha-aminoadipoyl)-(3R)-methyl-L-cysteine D-alpha-hydroxyisovaleryl ester (AmCOV) to probe the early stages of the catalytic cycle. The X-ray crystal structure of the anaerobic IPNS:Fe(II):AmCOV complex was solved to 1.40 A resolution, and it reveals several subtle differences in the active site relative to the complex of the enzyme with its natural substrate. The crystalline IPNS:Fe(II):AmCOV complex was then exposed to oxygen gas at high pressure; this brought about reaction to give what appears to be a hydroxymethyl/ene-thiol product. A mechanism for this reaction is proposed. These results offer further insight into the delicate interplay of steric and electronic effects in the IPNS active site and the mechanistic intricacies of this remarkable enzyme.
About this Structure
1W3V is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.
Reference
Unexpected oxidation of a depsipeptide substrate analogue in crystalline isopenicillin N synthase., Daruzzaman A, Clifton IJ, Adlington RM, Baldwin JE, Rutledge PJ, Chembiochem. 2006 Feb;7(2):351-8. PMID:16444759
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