1grr
From Proteopedia
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|PDB= 1grr |SIZE=350|CAPTION= <scene name='initialview01'>1grr</scene>, resolution 2.90Å | |PDB= 1grr |SIZE=350|CAPTION= <scene name='initialview01'>1grr</scene>, resolution 2.90Å | ||
|SITE= <scene name='pdbsite=SO4:Clc+Binding+Site+For+Chain+A'>SO4</scene> | |SITE= <scene name='pdbsite=SO4:Clc+Binding+Site+For+Chain+A'>SO4</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CLC:N-ACETYL-P-NITROPHENYLSERINOL'>CLC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1grr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1grr OCA], [http://www.ebi.ac.uk/pdbsum/1grr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1grr RCSB]</span> | ||
}} | }} | ||
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[[Category: Streptomyces venezuelae]] | [[Category: Streptomyces venezuelae]] | ||
[[Category: Izard, T.]] | [[Category: Izard, T.]] | ||
| - | [[Category: CLC]] | ||
| - | [[Category: SO4]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:49:58 2008'' |
Revision as of 17:50, 30 March 2008
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| , resolution 2.90Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
1GRR is a Single protein structure of sequence from Streptomyces venezuelae. 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
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