1qhs: Difference between revisions
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[[Image:1qhs.jpg|left|200px]] | [[Image:1qhs.jpg|left|200px]] | ||
'''CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE''' | {{Structure | ||
|PDB= 1qhs |SIZE=350|CAPTION= <scene name='initialview01'>1qhs</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CLM:CHLORAMPHENICOL'>CLM</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1QHS is a [ | 1QHS 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=1QHS OCA]. | ||
==Reference== | ==Reference== | ||
The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism., Izard T, Ellis J, EMBO J. 2000 Jun 1;19(11):2690-700. PMID:[http:// | The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism., Izard T, Ellis J, EMBO J. 2000 Jun 1;19(11):2690-700. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10835366 10835366] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces venezuelae]] | [[Category: Streptomyces venezuelae]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
''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 13:37:43 2008'' | ||
Revision as of 11:37, 20 March 2008
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| 1qhs, resolution 2.8Å | |||||||||||||
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| Ligands: | SO4 and CLM | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CHLORAMPHENICOL PHOSPHOTRANSFERASE IN COMPLEX WITH CHLORAMPHENICOL FROM STREPTOMYCES VENEZUELAE
Overview
Chloramphenicol (Cm), produced by the soil bacterium Streptomyces venezuelae, is an inhibitor of bacterial ribosomal peptidyltransferase activity. The Cm-producing streptomycete modifies the primary (C-3) hydroxyl of the antibiotic by a novel Cm-inactivating enzyme, chloramphenicol 3-O-phosphotransferase (CPT). Here we describe the crystal structures of CPT in the absence and presence of bound substrates. The enzyme is dimeric in a sulfate-free solution and tetramerization is induced by ammonium sulfate, the crystallization precipitant. The tetrameric quaternary structure exhibits crystallographic 222 symmetry and has ATP binding pockets located at a crystallographic 2-fold axis. Steric hindrance allows only one ATP to bind per dimer within the tetramer. In addition to active site binding by Cm, an electron-dense feature resembling the enzyme's product is found at the other subunit interface. The structures of CPT suggest that an aspartate acts as a general base to accept a proton from the 3-hydroxyl of Cm, concurrent with nucleophilic attack of the resulting oxyanion on the gamma-phosphate of ATP. Comparison between liganded and substrate-free CPT structures highlights side chain movements of the active site's Arg136 guanidinium group of >9 A upon substrate binding.
About this Structure
1QHS is a Single protein structure of sequence from Streptomyces venezuelae. Full crystallographic information is available from OCA.
Reference
The crystal structures of chloramphenicol phosphotransferase reveal a novel inactivation mechanism., Izard T, Ellis J, EMBO J. 2000 Jun 1;19(11):2690-700. PMID:10835366
Page seeded by OCA on Thu Mar 20 13:37:43 2008
