3IJP

Crystal structure of dihydrodipicolinate reductase from bartonella henselae at 2.0A resolution

Summary for 3IJP

• Entry DOI: 10.2210/pdb3ijp/pdb
• Descriptor: Dihydrodipicolinate reductase, SODIUM ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: ssgcid, sbri, decode biostructures, niaid, bartonella henselae, dihydrodipicolinate reductase, amino-acid biosynthesis, diaminopimelate biosynthesis, lysine biosynthesis, nadp, oxidoreductase, structural genomics, seattle structural genomics center for infectious disease
• Biological source: Bartonella henselae (Rochalimaea henselae)
• Cellular location: Cytoplasm : Q6G2G3
• Total number of polymer chains: 2
• Total formula weight: 62878.48

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2009-08-04, release date: 2009-08-11, Last modification date: 2023-09-06)

Primary citation

Cala, A.R.,Nadeau, M.T.,Abendroth, J.,Staker, B.L.,Reers, A.R.,Weatherhead, A.W.,Dobson, R.C.,Myler, P.J.,Hudson, A.O.
The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 angstrom resolution.
Acta Crystallogr F Struct Biol Commun, 72:885-891, 2016

PubMed Abstract: In bacteria, the second committed step in the diaminopimelate/lysine anabolic pathways is catalyzed by the enzyme dihydrodipicolinate reductase (DapB). DapB catalyzes the reduction of dihydrodipicolinate to yield tetrahydrodipicolinate. Here, the cloning, expression, purification, crystallization and X-ray diffraction analysis of DapB from the human-pathogenic bacterium Bartonella henselae, the causative bacterium of cat-scratch disease, are reported. Protein crystals were grown in conditions consisting of 5%(w/v) PEG 4000, 200 mM sodium acetate, 100 mM sodium citrate tribasic pH 5.5 and were shown to diffract to ∼2.3 Å resolution. They belonged to space group P422, with unit-cell parameters a = 109.38, b = 109.38, c = 176.95 Å. R was 0.11, R was 0.177 and R was 0.208. The three-dimensional structural features of the enzymes show that DapB from B. henselae is a tetramer consisting of four identical polypeptides. In addition, the substrate NADP was found to be bound to one monomer, which resulted in a closed conformational change in the N-terminal domain.

PubMed: 27917836
DOI: 10.1107/S2053230X16018525

Experimental method

X-RAY DIFFRACTION (2.3 Å)