3S4X
Crystal structure of the Asn152Gly mutant of P99 beta-lactamase
Summary for 3S4X
| Entry DOI | 10.2210/pdb3s4x/pdb |
| Descriptor | Beta-lactamase, SULFATE ION (3 entities in total) |
| Functional Keywords | hydrolase, cephalosporinase |
| Biological source | Enterobacter cloacae |
| Cellular location | Periplasm (By similarity): P05364 |
| Total number of polymer chains | 1 |
| Total formula weight | 40754.08 |
| Authors | Ruble, J.F.,Powers, R.A. (deposition date: 2011-05-20, release date: 2012-08-01, Last modification date: 2023-09-13) |
| Primary citation | Ruble, J.F.,Lefurgy, S.T.,Cornish, V.W.,Powers, R.A. Structural analysis of the Asn152Gly mutant of P99 cephalosporinase. Acta Crystallogr.,Sect.D, 68:1189-1193, 2012 Cited by PubMed Abstract: P99 cephalosporinase is a class C β-lactamase that is responsible in part for the widespread bacterial resistance to β-lactam antibiotics. Mutations of the conserved active-site residue Asn152 of the enzyme have been shown to alter β-lactam substrate specificity in vivo. Mutation of Asn152 to a glycine is notable in that it exhibits in vivo substrate-selectivity switching. In order to better understand the structural basis for this observed switch, the X-ray crystal structure of the apo Asn152Gly mutant of P99 was determined to 1.95 Å resolution. Unexpectedly, the artificial C-terminal His(6) tag of a symmetrically-related molecule was observed bound in the active site. The His(6) tag makes several interactions with key active-site residues, as well as with several sulfate ions. Additionally, the overall C-terminus occupies the space left vacant upon the mutation of Asn152 to glycine. PubMed: 22948919DOI: 10.1107/S0907444912024080 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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