Abstract
Escherichia coli tRNA N6-threonylcarbamoyladenosine dehydratase (TcdA), previously called CsdL or YgdL, was overproduced and purified from E. coli and crystallized using polyethylene glycol 3350 as a crystallizing agent. X-ray diffraction data were collected to 2.70 Å resolution under cryoconditions using synchrotron X-rays. The crystals belonged to space group P2₁, with unit-cell parameters a=65.4, b=96.8, c=83.3 Å, β=111.7°. According to the Matthews coefficient, the asymmetric unit may contain up to four subunits of the monomeric protein, with a crystal volume per protein mass (VM) of 2.12 Å3 Da(-1) and 42.1% solvent content.
Keywords:
CsdL; N6-threonylcarbamoyladenosine dehydratase; TcdA; tRNA hypermodification.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine / analogs & derivatives*
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Adenosine / biosynthesis
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Adenosine / chemistry
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Adenosine / genetics
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Amino Acid Sequence
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Crystallization
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Crystallography, X-Ray
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Escherichia coli / enzymology*
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Escherichia coli / genetics
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Escherichia coli Proteins / biosynthesis
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / genetics
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Molecular Sequence Data
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RNA, Transfer / biosynthesis
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RNA, Transfer / chemistry*
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RNA, Transfer / genetics
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Threonine Dehydratase / biosynthesis
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Threonine Dehydratase / chemistry*
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Threonine Dehydratase / genetics
Substances
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Escherichia coli Proteins
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N(6)-(N-threonylcarbonyl)adenosine
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RNA, Transfer
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Threonine Dehydratase
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Adenosine