Abstract
The cloning, expression, purification, crystallization and preliminary crystallographic analysis of glucose-1-phosphate uridylyltransferase (UgpG) from Sphingomonas elodea ATCC 31461 bound to glucose-1-phosphate are reported. Diffraction data sets were obtained from seven crystal forms in five different space groups, with highest resolutions ranging from 4.20 to 2.65 A. The phase problem was solved for a P2(1) crystal form using multiple isomorphous replacement with anomalous scattering from an osmium derivative and a SeMet derivative. The best native crystal in space group P2(1) has unit-cell parameters a = 105.5, b = 85.7, c = 151.8 A, beta = 105.2 degrees . Model building and refinement are currently under way.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Binding Sites / genetics
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Cloning, Molecular
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Crystallization
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Crystallography, X-Ray / methods
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Gene Expression Regulation, Bacterial
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Glucosephosphates / chemistry
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Glucosephosphates / genetics
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Glucosephosphates / metabolism*
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Sphingomonas / enzymology*
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Sphingomonas / genetics*
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Substrate Specificity / genetics
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UTP-Glucose-1-Phosphate Uridylyltransferase / biosynthesis
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UTP-Glucose-1-Phosphate Uridylyltransferase / chemistry*
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UTP-Glucose-1-Phosphate Uridylyltransferase / genetics
Substances
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Bacterial Proteins
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Glucosephosphates
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glucose-1-phosphate
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UTP-Glucose-1-Phosphate Uridylyltransferase