6UE0

Crystal structure of dihydrodipicolinate synthase from Klebsiella pneumoniae bound to pyruvate

This is a non-PDB format compatible entry.

Summary for 6UE0

• Entry DOI: 10.2210/pdb6ue0/pdb
• Descriptor: 4-hydroxy-tetrahydrodipicolinate synthase, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: dhdps, lysine biosynthesis, tetramer, lyase
• Biological source: Klebsiella pneumoniae
• Total number of polymer chains: 2
• Total formula weight: 70038.50

Authors

Impey, R.E.,Lee, M.,Hawkins, D.A.,Sutton, J.M.,Panjikar, S.,Perugini, M.A.,Soares da Costa, T.P. (deposition date: 2019-09-20, release date: 2020-02-05, Last modification date: 2023-11-29)

Primary citation

Impey, R.E.,Lee, M.,Hawkins, D.A.,Sutton, J.M.,Panjikar, S.,Perugini, M.A.,Soares da Costa, T.P.
Mis-annotations of a promising antibiotic target in high-priority gram-negative pathogens.
Febs Lett., 594:1453-1463, 2020

PubMed Abstract: The rise of antibiotic resistance combined with the lack of new products entering the market has led to bacterial infections becoming one of the biggest threats to global health. Therefore, there is an urgent need to identify novel antibiotic targets, such as dihydrodipicolinate synthase (DHDPS), an enzyme involved in the production of essential metabolites in cell wall and protein synthesis. Here, we utilised a 7-residue sequence motif to identify mis-annotation of multiple DHDPS genes in the high-priority Gram-negative bacteria Acinetobacter baumannii and Klebsiella pneumoniae. We subsequently confirmed these mis-annotations using a combination of enzyme kinetics and X-ray crystallography. Thus, this study highlights the need to ensure genes encoding promising drug targets, like DHDPS, are annotated correctly, especially for clinically important pathogens. PDB ID: 6UE0.

PubMed: 31943170
DOI: 10.1002/1873-3468.13733

Experimental method

X-RAY DIFFRACTION (1.892 Å)