3ML0
Thermostable Penicillin G acylase from Alcaligenes faecalis in tetragonal form
Summary for 3ML0
| Entry DOI | 10.2210/pdb3ml0/pdb |
| Related | 3K3W |
| Descriptor | Penicillin G acylase, alpha subunit, Penicillin G acylase, beta subunit, CALCIUM ION (3 entities in total) |
| Functional Keywords | penicillin g acylase, hydrolase |
| Biological source | Alcaligenes faecalis More |
| Total number of polymer chains | 2 |
| Total formula weight | 85090.92 |
| Authors | Varshney, N.K.,Kumar, R.S.,Ignatova, Z.,Dodson, E.,Suresh, C.G. (deposition date: 2010-04-16, release date: 2010-05-05, Last modification date: 2024-10-09) |
| Primary citation | Varshney, N.K.,Kumar, R.S.,Ignatova, Z.,Prabhune, A.,Pundle, A.,Dodson, E.,Suresh, C.G. Crystallization and X-ray structure analysis of a thermostable penicillin G acylase from Alcaligenes faecalis. Acta Crystallogr.,Sect.F, 68:273-277, 2012 Cited by PubMed Abstract: The enzyme penicillin G acylase (EC 3.5.1.11) catalyzes amide-bond cleavage in benzylpenicillin (penicillin G) to yield 6-aminopenicillanic acid, an intermediate chemical used in the production of semisynthetic penicillins. A thermostable penicillin G acylase from Alcaligenes faecalis (AfPGA) has been crystallized using the hanging-drop vapour-diffusion method in two different space groups: C222(1), with unit-cell parameters a = 72.9, b = 86.0, c = 260.2 , and P4(1)2(1)2, with unit-cell parameters a = b = 85.6, c = 298.8 . Data were collected at 293 and the structure was determined using the molecular-replacement method. Like other penicillin acylases, AfPGA belongs to the N-terminal nucleophilic hydrolase superfamily, has undergone post-translational processing and has a serine as the N-terminal residue of the β-chain. A disulfide bridge has been identified in the structure that was not found in the other two known penicillin G cylase structures. The presence of the disulfide bridge is perceived to be one factor that confers higher stability to this enzyme. PubMed: 22442220DOI: 10.1107/S1744309111053930 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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