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1w05
From Proteopedia
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|PDB= 1w05 |SIZE=350|CAPTION= <scene name='initialview01'>1w05</scene>, resolution 2.46Å | |PDB= 1w05 |SIZE=350|CAPTION= <scene name='initialview01'>1w05</scene>, resolution 2.46Å | ||
|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=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=W05:DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-D-ALANINE'>W05</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=1w05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w05 OCA], [http://www.ebi.ac.uk/pdbsum/1w05 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1w05 RCSB]</span> | ||
}} | }} | ||
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[[Category: Long, A J.]] | [[Category: Long, A J.]] | ||
[[Category: Rutledge, P J.]] | [[Category: Rutledge, P J.]] | ||
| - | [[Category: FE2]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: W05]] | ||
[[Category: b-lactam antibiotic]] | [[Category: b-lactam antibiotic]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| Line 34: | Line 34: | ||
[[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 00:29:17 2008'' |
Revision as of 21:29, 30 March 2008
| |||||||
| , resolution 2.46Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 AMINOADIPOYL-CYSTEINYL-ALANINE-FE COMPLEX
Overview
Isopenicillin N synthase (IPNS), a non-heme iron(II)-dependent oxidase, catalyzes conversion of the tripeptide delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-valine (ACV) to bicyclic isopenicillin N (IPN), concomitant with the reduction of dioxygen to two molecules of water. Incubation of the "truncated"substrate analogues delta-(l-alpha-aminoadipoyl)-l-cysteinyl-glycine (ACG) and delta-(l-alpha-aminoadipoyl)-l-cysteinyl-d-alanine (ACA) with IPNS has previously been shown to afford acyclic products, in which the substrate cysteinyl residue has undergone a two-electron oxidation. We report X-ray crystal structures for the anaerobic IPNS/Fe(II)/ACG and IPNS/Fe(II)/ACA complexes, both in the absence and presence of the dioxygen analogue nitric oxide. The overall protein structures are very similar to those of the corresponding IPNS/Fe(II)/ACV complexes; however, significant differences are apparent in the vicinity of the active site iron. The structure of the IPNS/Fe(II)/ACG complex reveals that the C-terminal carboxylate of this substrate is oriented toward the active site iron atom, apparently hydrogen-bonded to an additional water ligand at the metal; this is a different binding mode to that observed in the IPNS/Fe(II)/ACV complex. ACA binds to the metal in a manner that is intermediate between those observed for ACV and ACG. The addition of NO to these complexes initiates conformational changes such that both the IPNS/Fe(II)/ACG/NO and IPNS/Fe(II)/ACA/NO structures closely resemble the IPNS/Fe(II)/ACV/NO complex. These results further demonstrate the feasibility of metal-centered rearrangements in catalysis by non-heme iron enzymes and provide insight into the delicate balance between hydrophilic-hydrophobic interactions and steric effects in the IPNS active site.
About this Structure
1W05 is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.
Reference
Structural studies on the reaction of isopenicillin N synthase with the truncated substrate analogues delta-(L-alpha-aminoadipoyl)-L-cysteinyl-glycine and delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-alanine., Long AJ, Clifton IJ, Roach PL, Baldwin JE, Rutledge PJ, Schofield CJ, Biochemistry. 2005 May 3;44(17):6619-28. PMID:15850395
Page seeded by OCA on Mon Mar 31 00:29:17 2008
