5UGV

DapB from Mycobacterium tuberculosis

Summary for 5UGV

• Entry DOI: 10.2210/pdb5ugv/pdb
• Descriptor: 4-hydroxy-tetrahydrodipicolinate reductase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, SULFATE ION, ... (5 entities in total)
• Functional Keywords: lysine biosynthesis, dapb, oxidoreductase
• Biological source: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
• Cellular location: Cytoplasm : A5U6C6
• Total number of polymer chains: 2
• Total formula weight: 58769.83

Authors

Pote, S.P.,Mank, N.,Chruszcz, M. (deposition date: 2017-01-10, release date: 2018-01-17, Last modification date: 2023-10-04)

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 (2.25 Å)