1w04: Difference between revisions
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[[Image:1w04.gif|left|200px]] | [[Image:1w04.gif|left|200px]] | ||
'''ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL-GLYCINE-FE-NO COMPLEX''' | {{Structure | ||
|PDB= 1w04 |SIZE=350|CAPTION= <scene name='initialview01'>1w04</scene>, resolution 1.28Å | |||
|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>, <scene name='pdbligand=HCG:DELTA-(L-ALPHA-AMINOADIPOYL)-L-CYSTEINYL-GLYCINE'>HCG</scene> and <scene name='pdbligand=NO:NITROGEN OXIDE'>NO</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] | |||
|GENE= | |||
}} | |||
'''ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL-GLYCINE-FE-NO COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1W04 is a [ | 1W04 is a [[Single protein]] 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=1W04 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15850395 15850395] | ||
[[Category: Emericella nidulans]] | [[Category: Emericella nidulans]] | ||
[[Category: Isopenicillin-N synthase]] | [[Category: Isopenicillin-N synthase]] | ||
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[[Category: penicillin biosynthesis]] | [[Category: penicillin biosynthesis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:50:17 2008'' | ||
Revision as of 15:50, 20 March 2008
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| , resolution 1.28Å | |||||||
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| Sites: | |||||||
| Ligands: | , , and | ||||||
| Activity: | Isopenicillin-N synthase, with EC number 1.21.3.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ISOPENICILLIN N SYNTHASE AMINOADIPOYL-CYSTEINYL-GLYCINE-FE-NO COMPLEX
OverviewOverview
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 StructureAbout this Structure
1W04 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 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
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