1grr: Difference between revisions

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|PDB= 1grr |SIZE=350|CAPTION= <scene name='initialview01'>1grr</scene>, resolution 2.90&Aring;
|PDB= 1grr |SIZE=350|CAPTION= <scene name='initialview01'>1grr</scene>, resolution 2.90&Aring;
|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=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CLC:N-ACETYL-P-NITROPHENYLSERINOL'>CLC</scene>
|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]]


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''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

File:1grr.jpg


Drag the structure with the mouse to rotate
1grr, resolution 2.90Å
Sites: SO4
Ligands: CLC, SO4
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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