دورية أكاديمية
Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family.
| العنوان: | Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family. |
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| المؤلفون: | Bompard-Gilles, C., Remaut, H., Villeret, V., Prange, T., Fanuel, L., Delmarcelle, Michaël, Joris, Bernard, Frère, Jean-Marie, Van Beeumen, J. |
| المصدر: | Structure, 8 (9), 971-80 (2000) |
| بيانات النشر: | Cell Press |
| سنة النشر: | 2000 |
| المجموعة: | University of Liège: ORBi (Open Repository and Bibliography) |
| مصطلحات موضوعية: | Amino Acid Sequence, Aminopeptidases/chemistry, Bacillus/enzymology, Bacterial Proteins, Binding Sites, Carboxypeptidases/chemistry, Carrier Proteins/chemistry, Crystallography, X-Ray, Dimerization, Hexosyltransferases, Models, Molecular, Molecular Sequence Data, Muramoylpentapeptide Carboxypeptidase/chemistry, Ochrobactrum anthropi/enzymology, Penicillin-Binding Proteins, Peptidyl Transferases, Protein Structure, Secondary, Streptomyces/enzymology, beta-Lactamases/chemistry, Life sciences, Biochemistry, biophysics & molecular biology, Sciences du vivant, Biochimie, biophysique & biologie moléculaire |
| الوصف: | peer reviewed ; BACKGROUND: beta-Lactam compounds are the most widely used antibiotics. They inactivate bacterial DD-transpeptidases, also called penicillin-binding proteins (PBPs), involved in cell-wall biosynthesis. The most common bacterial resistance mechanism against beta-lactam compounds is the synthesis of beta-lactamases that hydrolyse beta-lactam rings. These enzymes are believed to have evolved from cell-wall DD-peptidases. Understanding the biochemical and mechanistic features of the beta-lactam targets is crucial because of the increasing number of resistant bacteria. DAP is a D-aminopeptidase produced by Ochrobactrum anthropi. It is inhibited by various beta-lactam compounds and shares approximately 25% sequence identity with the R61 DD-carboxypeptidase and the class C beta-lactamases. RESULTS: The crystal structure of DAP has been determined to 1.9 A resolution using the multiple isomorphous replacement (MIR) method. The enzyme folds into three domains, A, B and C. Domain A, which contains conserved catalytic residues, has the classical fold of serine beta-lactamases, whereas domains B and C are both antiparallel eight-stranded beta barrels. A loop of domain C protrudes into the substrate-binding site of the enzyme. CONCLUSIONS: Comparison of the biochemical properties and the structure of DAP with PBPs and serine beta-lactamases shows that although the catalytic site of the enzyme is very similar to that of beta-lactamases, its substrate and inhibitor specificity rests on residues of domain C. DAP is a new member of the family of penicillin-recognizing proteins (PRPs) and, at the present time, its enzymatic specificity is clearly unique. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| تدمد: | 0969-2126 1878-4186 |
| العلاقة: | urn:issn:0969-2126; urn:issn:1878-4186; https://orbi.uliege.be/handle/2268/64021Test; info:hdl:2268/64021; scopus-id:2-s2.0-0034665239; info:pmid:10986464 |
| DOI: | 10.1016/S0969-2126(00)00188-X |
| الإتاحة: | https://doi.org/10.1016/S0969-2126Test(00)00188-X https://orbi.uliege.be/handle/2268/64021Test |
| رقم الانضمام: | edsbas.CD4DBF15 |
| قاعدة البيانات: | BASE |
Full Text Finder | تدمد: | 09692126 18784186 |
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| DOI: | 10.1016/S0969-2126(00)00188-X |