1grr: Difference between revisions

Revision as of 05:58, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1grr.png

Template:STRUCTURE 1grr

CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH 2-NAC-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAECHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH 2-NAC-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE

Template:ABSTRACT PUBMED 11468347

About this StructureAbout this Structure

1GRR is a Single protein structure of sequence from Streptomyces venezuelae. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity., Izard T, Protein Sci. 2001 Aug;10(8):1508-13. PMID:11468347

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OCA

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-'''CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH 2-NAC-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE'''
+===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 binds to the secondary product binding site.
+The line below this paragraph, {{ABSTRACT_PUBMED_11468347}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11468347}}
 ==About this Structure==
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 [[Category: Phosphorylation]]
 [[Category: Transferase]]
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