1GRR
CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH 2-Nac-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE
Summary for 1GRR
| Entry DOI | 10.2210/pdb1grr/pdb |
| Related | 1GRQ 1QHN 1QHS 1QHX 1QHY |
| Descriptor | CHLORAMPHENICOL 3-O PHOSPHOTRANSFERASE, SULFATE ION, N-ACETYL-P-NITROPHENYLSERINOL, ... (4 entities in total) |
| Functional Keywords | transferase, kinase, antibiotic resistance, phosphorylation, mononucleotide binding fold |
| Biological source | STREPTOMYCES VENEZUELAE |
| Total number of polymer chains | 1 |
| Total formula weight | 19184.67 |
| Authors | Izard, T. (deposition date: 2001-12-15, release date: 2002-01-04, Last modification date: 2023-12-13) |
| Primary citation | Izard, T. Structural Basis for Chloramphenicol Tolerance in Streptomyces Venezuelae by Chloramphenicol Phosphotransferase Activity Protein Sci., 10:1508-, 2001 Cited by PubMed Abstract: Streptomyces venezuelae synthesizes chloramphenicol (Cm), an inhibitor of ribosomal peptidyl transferase activity, thereby inhibiting bacterial growth. The producer escapes autoinhibition by its own secondary metabolite through phosphorylation of Cm by chloramphenicol phosphotransferase (CPT). In addition to active site binding, CPT binds its product 3-phosphoryl-Cm, in an alternate product binding site. To address the mechanisms of Cm tolerance of the producer, the crystal structures of CPT were determined in complex with either the nonchlorinated Cm (2-N-Ac-Cm) at 3.1 A resolution or the antibiotic's immediate precursor, the p-amino analog p-NH(2)-Cm, at 2.9 A resolution. Surprisingly, p-NH(2)-Cm binds CPT in a novel fashion. Additionally, neither 2-N-Ac-Cm nor p-NH(2)-Cm binds to the secondary product binding site. PubMed: 11468347DOI: 10.1110/PS.10.8.1508 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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