2oqc
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= | |LIGAND= | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Penicillin_amidase Penicillin amidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.11 3.5.1.11] </span> |
|GENE= yxeI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | |GENE= yxeI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2oqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oqc OCA], [http://www.ebi.ac.uk/pdbsum/2oqc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2oqc RCSB]</span> | ||
}} | }} | ||
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[[Category: penicillin v acylase]] | [[Category: penicillin v acylase]] | ||
| - | ''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 04:21:37 2008'' |
Revision as of 01:21, 31 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | yxeI (Bacillus subtilis) | ||||||
| Activity: | Penicillin amidase, with EC number 3.5.1.11 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Penicillin V acylase from Bacillus subtilis
Overview
Penicillin acylase proteins are amidohydrolase enzymes that cleave penicillins at the amide bond connecting the side chain to their beta-lactam nucleus. An unannotated protein from Bacillus subtilis has been expressed in Escherichia coli, purified and confirmed to possess penicillin V acylase activity. The protein was crystallized using the hanging-drop vapour-diffusion method from a solution containing 4 M sodium formate in 100 mM Tris-HCl buffer pH 8.2. Diffraction data were collected under cryogenic conditions to a spacing of 2.5 A. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 111.0, b = 308.0, c = 56.0 A. The estimated Matthews coefficient was 3.23 A3 Da(-1), corresponding to 62% solvent content. The structure has been solved using molecular-replacement methods with B. sphaericus penicillin V acylase (PDB code 2pva) as the search model.
About this Structure
2OQC is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Cloning, purification, crystallization and preliminary structural studies of penicillin V acylase from Bacillus subtilis., Rathinaswamy P, Pundle AV, Prabhune AA, Sivaraman H, Brannigan JA, Dodson GG, Suresh CG, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt, 7):680-3. Epub 2005 Jun 15. PMID:16511127
Page seeded by OCA on Mon Mar 31 04:21:37 2008
Categories: Bacillus subtilis | Penicillin amidase | Single protein | Brannigan, J A. | Dodson, G G. | Prabhune, A A. | Pundle, A V. | Rathinaswamy, P. | Sivaraman, H. | Suresh, C G. | Bacillus subtili | Choloylglycine hydrolase | Conjugated bile acid hydrolase | Ntn-hydrolase | Penicillin v acylase
