1qhn
From Proteopedia
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| - | [[Image:1qhn.jpg|left|200px]] | + | [[Image:1qhn.jpg|left|200px]] |
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| - | '''CHLORAMPHENICOL PHOSPHOTRANSFERASE FROM STREPTOMYCES VENEZUELAE''' | + | {{Structure |
| + | |PDB= 1qhn |SIZE=350|CAPTION= <scene name='initialview01'>1qhn</scene>, resolution 2.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CHLORAMPHENICOL PHOSPHOTRANSFERASE FROM STREPTOMYCES VENEZUELAE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QHN is a [ | + | 1QHN 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=1QHN 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 13:37:37 2008'' |
Revision as of 11:37, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHLORAMPHENICOL PHOSPHOTRANSFERASE 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
1QHN 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 13:37:37 2008
