5US6

Structure of Dihydrodipicolinate Reductase from Vibrio vulnificus Bound to NADH and 2,6 Pyridine Dicarboxylic Acid with Intact Polyhistidine Tag

Summary for 5US6

• Entry DOI: 10.2210/pdb5us6/pdb
• Descriptor: 4-hydroxy-tetrahydrodipicolinate reductase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PYRIDINE-2,6-DICARBOXYLIC ACID, ... (5 entities in total)
• Functional Keywords: lysine biosynthesis, oxidoreductase
• Biological source: Vibrio vulnificus
• Cellular location: Cytoplasm : Q8DEM0
• Total number of polymer chains: 12
• Total formula weight: 386863.61

Authors

Mank, N.M.,Arnette, A.K.,Chruszcz, M. (deposition date: 2017-02-13, release date: 2018-02-21, Last modification date: 2024-03-06)

Primary citation

Pote, S.,Kachhap, S.,Mank, N.J.,Daneshian, L.,Klapper, V.,Pye, S.,Arnette, A.K.,Shimizu, L.S.,Borowski, T.,Chruszcz, M.
Comparative structural and mechanistic studies of 4-hydroxy-tetrahydrodipicolinate reductases from Mycobacterium tuberculosis and Vibrio vulnificus.
Biochim Biophys Acta Gen Subj, 1865:129750-129750, 2021

PubMed Abstract: The products of the lysine biosynthesis pathway, meso-diaminopimelate and lysine, are essential for bacterial survival. This paper focuses on the structural and mechanistic characterization of 4-hydroxy-tetrahydrodipicolinate reductase (DapB), which is one of the enzymes from the lysine biosynthesis pathway. DapB catalyzes the conversion of (2S, 4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate (HTPA) to 2,3,4,5-tetrahydrodipicolinate in an NADH/NADPH dependent reaction. Genes coding for DapBs were identified as essential for many pathogenic bacteria, and therefore DapB is an interesting new target for the development of antibiotics.

PubMed: 32980502
DOI: 10.1016/j.bbagen.2020.129750

Experimental method

X-RAY DIFFRACTION (2.61 Å)