1oc1: Difference between revisions
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|PDB= 1oc1 |SIZE=350|CAPTION= <scene name='initialview01'>1oc1</scene>, resolution 2.20Å | |PDB= 1oc1 |SIZE=350|CAPTION= <scene name='initialview01'>1oc1</scene>, resolution 2.20Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Chain+A'>AC1</scene> | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=ASV:DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-VINYLGLYCINE'>ASV</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oc1 OCA], [http://www.ebi.ac.uk/pdbsum/1oc1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1oc1 RCSB]</span> | |||
}} | }} | ||
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[[Category: Rutledge, P J.]] | [[Category: Rutledge, P J.]] | ||
[[Category: Schofield, C J.]] | [[Category: Schofield, C J.]] | ||
[[Category: b-lactam antibiotic]] | [[Category: b-lactam antibiotic]] | ||
[[Category: oxygenase]] | [[Category: oxygenase]] | ||
[[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 Sun Mar 30 22:43:02 2008'' | ||
Revision as of 22:43, 30 March 2008
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| , resolution 2.20Å | |||||||
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| Sites: | |||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL-AMINOBUTYRATE-FE COMPLEX
OverviewOverview
Isopenicillin N synthase (IPNS) is a non-haem iron(II) oxidase which catalyses the biosynthesis of isopenicillin N from the tripeptide delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-valine (ACV). Herein we report crystallographic studies to investigate the reaction of IPNS with the truncated substrate analogue delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alpha-aminobutyrate (ACAb). It has been reported previously that this analogue gives rise to three beta-lactam products when incubated with IPNS: two methyl penams and a cepham. Crystal structures of the IPNS-Fe(II)-ACAb and IPNS-Fe(II)-ACAb-NO complexes have now been solved and are reported herein. These structures and modelling studies based on them shed light on the diminished product selectivity shown by IPNS in its reaction with ACAb and further rationalize the presence of certain key residues at the IPNS active site.
About this StructureAbout this Structure
1OC1 is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.
ReferenceReference
Structural studies on the reaction of isopenicillin N synthase with the substrate analogue delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alpha-aminobutyrate., Long AJ, Clifton IJ, Roach PL, Baldwin JE, Schofield CJ, Rutledge PJ, Biochem J. 2003 Jun 15;372(Pt 3):687-93. PMID:12622704
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