Premium
The crystal structure of dihydrodipicolinate synthase from Escherichia coli with bound pyruvate and succinic acid semialdehyde: Unambiguous resolution of the stereochemistry of the condensation product
Author(s) -
Boughton Berin A.,
Dobson Renwick C. J.,
Hutton Craig A.
Publication year - 2012
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24106
Subject(s) - active site , chemistry , stereochemistry , escherichia coli , aldol condensation , substrate (aquarium) , atp synthase , protein data bank (rcsb pdb) , crystal structure , crystallography , enzyme , biochemistry , biology , catalysis , ecology , gene
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. Proteins 2012; © 2012 Wiley Periodicals, Inc.