Abstract | BACKGROUND: RESULTS: The first three-dimensional structure of the enzyme was determined at 1.4 A resolution using the multiwavelength anomalous diffraction (MAD) method on Escherichia coli protein crystals containing gold. The protein consists of an alpha + beta fold having a complex linkage of beta strands. Intersubunit contacts are mediated by numerous hydrophobic interactions and three hydrogen bond networks. CONCLUSIONS: A proposed active site was identified on the basis of amino acid residues that are conserved among the enzyme from 19 species. There are two well-separated active sites per dimer, each of which comprise residues from both subunits. In addition to three arginines and two threonines, which may be used for recognizing the phosphate group of the substrate, the active site consists of three glutamates, two aspartates, two histidines, and a cysteine which may provide the means for general acid and base catalysis and for coordinating the Mg(2+) cofactor within the active site.
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Authors | D I Liao, J C Calabrese, Z Wawrzak, P V Viitanen, D B Jordan |
Journal | Structure (London, England : 1993)
(Structure)
Vol. 9
Issue 1
Pg. 11-8
(Jan 10 2001)
ISSN: 0969-2126 [Print] United States |
PMID | 11342130
(Publication Type: Journal Article)
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Chemical References |
- Aspartic Acid
- Glutamic Acid
- Histidine
- Riboflavin Synthase
- Intramolecular Transferases
- L-3,4-dihydroxy-2-butanone-4-phosphate synthase
- Magnesium
- Cysteine
- Riboflavin
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Topics |
- Aspartic Acid
(chemistry)
- Binding Sites
- Catalysis
- Crystallography, X-Ray
- Cysteine
(chemistry)
- Dimerization
- Escherichia coli
(enzymology)
- Glutamic Acid
(chemistry)
- Histidine
(chemistry)
- Intramolecular Transferases
(chemistry)
- Magnesium
(chemistry)
- Models, Chemical
- Models, Molecular
- Protein Structure, Secondary
- Riboflavin
(biosynthesis, chemistry)
- Riboflavin Synthase
(chemistry)
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