1grr: Difference between revisions
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'''CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH 2-NAC-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE''' | {{Structure | ||
|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> | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CLC:N-ACETYL-P-NITROPHENYLSERINOL'>CLC</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH 2-NAC-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GRR is a [ | 1GRR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GRR OCA]. | ||
==Reference== | ==Reference== | ||
Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity., Izard T, Protein Sci. 2001 Aug;10(8):1508-13. PMID:[http:// | Structural basis for chloramphenicol tolerance in Streptomyces venezuelae by chloramphenicol phosphotransferase activity., Izard T, Protein Sci. 2001 Aug;10(8):1508-13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11468347 11468347] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces venezuelae]] | [[Category: Streptomyces venezuelae]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:27:03 2008'' | ||
Revision as of 12:27, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH 2-NAC-CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE
OverviewOverview
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 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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