1ips: Difference between revisions
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[[Image:1ips.jpg|left|200px]] | [[Image:1ips.jpg|left|200px]] | ||
'''ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)''' | {{Structure | ||
|PDB= 1ips |SIZE=350|CAPTION= <scene name='initialview01'>1ips</scene>, resolution 2.5Å | |||
|SITE= <scene name='pdbsite=SA:Active+Site+(Mn+Binding),+A+Chain'>SA</scene> and <scene name='pdbsite=SB:Active+Site+(Mn+Binding),+B+Chain'>SB</scene> | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE (II) ION'>MN</scene> | |||
|ACTIVITY= | |||
|GENE= PCB C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=162425 Emericella nidulans]) | |||
}} | |||
'''ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1IPS is a [ | 1IPS 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=1IPS OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes., Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE, Nature. 1995 Jun 22;375(6533):700-4. PMID:[http:// | Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes., Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE, Nature. 1995 Jun 22;375(6533):700-4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7791906 7791906] | ||
[[Category: Emericella nidulans]] | [[Category: Emericella nidulans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 11:53:22 2008'' | ||
Revision as of 09:53, 20 March 2008
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| 1ips, resolution 2.5Å | |||||||||||||
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| Sites: | SA and SB | ||||||||||||
| Ligands: | MN | ||||||||||||
| Gene: | PCB C (Emericella nidulans) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)
Overview
Penicillin antibiotics are all produced from fermentation-derived penicillins because their chemical synthesis is not commercially viable. The key step in penicillin biosynthesis, in which both the beta-lactam and thiazolidine rings of the nucleus are created, is mediated by isopenicillin N synthase (IPNS), which binds ferrous iron and uses dioxygen as a cosubstrate. In a unique enzymatic step, with no chemical precedent, IPNS catalyses the transfer of four hydrogen atoms from its tripeptide substrate to dioxygen forming, in a single reaction, the complete bicyclic nucleus of the penicillins. We now report the structure of IPNS complexed with manganese, which reveals the active site is unusually buried within a 'jelly-roll' motif and lined by hydrophobic residues, and suggest how this structure permits the process of penicillin formation. Sequence analyses indicate IPNS, 1-aminocyclopropane-1-carboxylic acid oxidase and many of the 2-oxo-acid-dependent oxygenases contain a conserved jelly-roll motif, forming a new structural family of enzymes.
About this Structure
1IPS is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.
Reference
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes., Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE, Nature. 1995 Jun 22;375(6533):700-4. PMID:7791906
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