1grr
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(New page: 200px<br /> <applet load="1grr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1grr, resolution 2.90Å" /> '''CHLORAMPHENICOL PHO...)
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Revision as of 18:32, 29 October 2007
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CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH 2-NAC-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE
Overview
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 ... [(full description)]
About this Structure
1GRR is a [Single protein] structure of sequence from [Streptomyces venezuelae] with SO4 and CLC as [ligands]. Full crystallographic information is available from [OCA].
Reference
Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity., Izard T, Protein Sci. 2001 Aug;10(8):1508-13. PMID:11468347
Page seeded by OCA on Mon Oct 29 20:37:03 2007
