3WWL

Crystal structure of lysine biosynthetic amino acid carrier protein LysW from Thermus thermophilus conjugated with alpha-aminoadipate

Summary for 3WWL

• Entry DOI: 10.2210/pdb3wwl/pdb
• Related: 3WWM 3WWN
• Descriptor: Alpha-aminoadipate carrier protein LysW, ZINC ION (3 entities in total)
• Functional Keywords: zinc finger, amino acid carrier protein, metal binding protein
• Biological source: Thermus thermophilus HB27
• Total number of polymer chains: 1
• Total formula weight: 6022.99

Authors

Yoshida, A.,Tomita, T.,Kuzuyama, T.,Nishiyama, M. (deposition date: 2014-06-21, release date: 2014-11-19, Last modification date: 2023-11-15)

Primary citation

Yoshida, A.,Tomita, T.,Fujimura, T.,Nishiyama, C.,Kuzuyama, T.,Nishiyama, M.
Structural insight into amino group-carrier protein-mediated lysine biosynthesis: crystal structure of the LysZ·LysW complex from Thermus thermophilus.
J.Biol.Chem., 290:435-447, 2015

PubMed Abstract: In the biosynthesis of lysine by Thermus thermophilus, the metabolite α-ketoglutarate is converted to the intermediate α-aminoadipate (AAA), which is protected by the 54-amino acid acidic protein LysW. In this study, we determined the crystal structure of LysZ from T. thermophilus (TtLysZ), an amino acid kinase that catalyzes the second step in the AAA to lysine conversion, which was in a complex with LysW at a resolution of 1.85 Å. A crystal analysis coupled with isothermal titration calorimetry of the TtLysZ mutants for TtLysW revealed tight interactions between LysZ and the globular and C-terminal extension domains of the LysW protein, which were mainly attributed to electrostatic forces. These results provided structural evidence for LysW acting as a protecting molecule for the α-amino group of AAA and also as a carrier protein to guarantee better recognition by biosynthetic enzymes for the efficient biosynthesis of lysine.

PubMed: 25392000
DOI: 10.1074/jbc.M114.595983

Experimental method

X-RAY DIFFRACTION (1.2 Å)