6ue0

Crystal structure of dihydrodipicolinate synthase from Klebsiella pneumoniae bound to pyruvate

spinqualitylabelsall models 6ue0, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ue0 is a 2 chain structure with sequence from Klebsiella pneumoniae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.892Å Ligands: CL, KPI, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W9BBZ5_KLEPN Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418][SAAS:SAAS00570606] Publication Abstract from PubMed 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. Mis-annotations of a promising antibiotic target in high-priority gram-negative pathogens.,Impey RE, Lee M, Hawkins DA, Sutton JM, Panjikar S, Perugini MA, Soares da Costa TP FEBS Lett. 2020 Jan 13. doi: 10.1002/1873-3468.13733. PMID:31943170 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dihydrodipicolinate synthase

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