1qhs
From Proteopedia
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|PDB= 1qhs |SIZE=350|CAPTION= <scene name='initialview01'>1qhs</scene>, resolution 2.8Å | |PDB= 1qhs |SIZE=350|CAPTION= <scene name='initialview01'>1qhs</scene>, resolution 2.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CLM:CHLORAMPHENICOL'>CLM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1qhn|1QHN]], [[1qhs|1QHS]], [[1qhx|1QHX]], [[1qhy|1QHY]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qhs OCA], [http://www.ebi.ac.uk/pdbsum/1qhs PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qhs RCSB]</span> | ||
}} | }} | ||
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[[Category: Streptomyces venezuelae]] | [[Category: Streptomyces venezuelae]] | ||
[[Category: Izard, T.]] | [[Category: Izard, T.]] | ||
| - | [[Category: CLM]] | ||
| - | [[Category: SO4]] | ||
[[Category: antibiotic resistance]] | [[Category: antibiotic resistance]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
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[[Category: phosphorylation]] | [[Category: phosphorylation]] | ||
| - | ''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 23:13:45 2008'' |
Revision as of 20:13, 30 March 2008
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| , resolution 2.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1QHN, 1QHS, 1QHX, 1QHY
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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