5TJZ

Structure of 4-Hydroxytetrahydrodipicolinate Reductase from Mycobacterium tuberculosis with NADPH and 2,6 Pyridine Dicarboxylic Acid

Summary for 5TJZ

• Entry DOI: 10.2210/pdb5tjz/pdb
• Related: 5TJY
• Descriptor: 4-hydroxy-tetrahydrodipicolinate reductase, PYRIDINE-2,6-DICARBOXYLIC ACID, BENZOIC ACID, ... (10 entities in total)
• Functional Keywords: oxidoreductase, lysine biosynthesis
• Biological source: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)
• Cellular location: Cytoplasm : A5U6C6
• Total number of polymer chains: 1
• Total formula weight: 27679.20

Authors

Mank, N.J.,Arnette, A.K.,Klapper, V.,Chruszcz, M. (deposition date: 2016-10-05, release date: 2018-01-10, 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 (1.5 Å)