5XTF

Crystal structure of the cis-dihydrodiol naphthalene dehydrogenase NahB from Pseudomonas sp. MC1

5XTF の概要

• エントリーDOI: 10.2210/pdb5xtf/pdb
• 分子名称: 2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase (2 entities in total)
• 機能のキーワード: tetramer, cis-dihydrodiol naphthalene dehydrogenase, oxidoreductase
• 由来する生物種: Pseudomonas sp. MC1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59642.47

構造登録者

Park, A.K.,Kim, H.-W. (登録日: 2017-06-19, 公開日: 2017-08-09, 最終更新日: 2023-11-22)

主引用文献

Park, A.K.,Kim, H.,Kim, I.S.,Roh, S.J.,Shin, S.C.,Lee, J.H.,Park, H.,Kim, H.W.
Crystal structure of cis-dihydrodiol naphthalene dehydrogenase (NahB) from Pseudomonas sp. MC1: Insights into the early binding process of the substrate
Biochem. Biophys. Res. Commun., 491:403-408, 2017

PubMed Abstract: The bacterial strain Pseudomonas sp. MC1 harbors an 81-kb metabolic plasmid, which encodes enzymes involved in the conversion of naphthalene to salicylate. Of these, the enzyme NahB (cis-dihydrodiol naphthalene dehydrogenase), which catalyzes the second reaction of this pathway, binds to various substrates such as cis-1,2-dihydro-1,2-dihydroxy-naphthalene (1,2-DDN), cis-2,3-dihydro-2,3-dihydroxybiphenyl (2,3-DDB), and 3,4-dihydro-3,4-dihydroxy-2,2',5,5'-tetrachlorobiphenyl (3,4-DD-2,2',5-5-TCB). However, the mechanism underlying its broad substrate specificity is unclear owing to the lack of structural information. Here, we determined the first crystal structures of NahB in the absence and presence of NAD and 2,3-dihydroxybiphenyl (2,3-DB). Structure analysis suggests that the flexible substrate-binding loop allows NahB to accommodate diverse substrates. Furthermore, we defined the initial steps of substrate recognition and identified the early substrate-binding site in the substrate recognition process through the complex structure with ligands.

PubMed: 28728845
DOI: 10.1016/j.bbrc.2017.07.089

実験手法

X-RAY DIFFRACTION (2.095 Å)