J Mol Biol. 1994 Jan 14;235(2):774-6.

Sequence and crystallization of Escherichia coli dethiobiotin synthetase, the penultimate enzyme of biotin biosynthesis.

Alexeev D, Bury SM, Boys CW, Turner MA, Sawyer L, Ramsey AJ, Baxter HC, Baxter RL.

Source

Department of Biochemistry, University of Edinburgh, Scotland.

Abstract

The enzyme dethiobiotin synthetase (EC 6.3.3.3) has been cloned and over-expressed in Escherichia coli in such a way that milligram quantities are available. The purified enzyme has been subjected to a number of physical and chemical studies, sequenced and most notably it has been crystallized in a form that is suitable for X-ray structure determination. The cell dimensions are a = 72.8 A, b = 49.2 A, c = 61.4 A, beta = 106.2 degrees. The systematic absences are consistent with the monoclinic space group C2 with one polypeptide chain in the asymmetric unit.

PMID:: 8289297; [PubMed - indexed for MEDLINE]

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Research Support, Non-U.S. Gov't

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GENBANK/S68059

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Structures reported by this article

Mechanistic Implications And Family Relationships From The Structure Of Dethiobiotin Synthetase

PDB: 1DBS

Source: Escherichia coli

Method: X-Ray Diffraction

Resolution: 1.8 Å

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J Mol Biol. 1994 Jan 14 ;235(2):774-6.

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