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The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semi-aldehyde: Unambiguous resolution of the stereochemistry of the condensation product
Journal article   Peer reviewed

The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semi-aldehyde: Unambiguous resolution of the stereochemistry of the condensation product

B.A. Boughton, R.C.J. Dobson and C.A. Hutton
Proteins: Structure, Function, and Bioinformatics, Vol.80(8), pp.2117-2122
2012
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Abstract

The crystal structure of Escherichia coli dihydrodipicolinate synthase with pyruvate and substrate analogue succinic acid semialdehyde condensed with the active site lysine‐161 was solved to a resolution of 2.3 Å. Comparative analysis to a previously reported structure both resolves the configuration at the aldol addition center, where the final addition product clearly displays the (S )‐configuration, and the final conformation of the adduct within the active site. Direct comparison to two other crystal structures found in the Protein Data Bank, 1YXC, and 3DU0, demonstrates significant similarity between the active site residues of these structures.

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Collaboration types
Domestic collaboration
International collaboration
Citation topics
3 Agriculture, Environment & Ecology
3.180 Microbial Biotechnology
3.180.1184 Amino Acid Biosynthesis
Web Of Science research areas
Biochemistry & Molecular Biology
Biophysics
ESI research areas
Biology & Biochemistry
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