1grr: Difference between revisions

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==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.

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.

==About this Structure==

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[[Category: transferase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:17 2008''

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@@ Line 4: / Line 4: @@
 ==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.
+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.
 ==About this Structure==
@@ Line 22: / Line 22: @@
 [[Category: transferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:42:07 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:53:17 2008''