5JC6

Carboxypeptidase B with 2-nd zinc and acetate ion

5JC6 の概要

• エントリーDOI: 10.2210/pdb5jc6/pdb
• 分子名称: Carboxypeptidase B, ZINC ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: hydrolase
• 由来する生物種: Sus scrofa (Pig)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34923.75

構造登録者

Timofeev, V.I.,Akparov, V.K.,Kuranova, I.P. (登録日: 2016-04-14, 公開日: 2017-05-24, 最終更新日: 2024-10-23)

主引用文献

Akparov, V.,Timofeev, V.,Khaliullin, I.,Svedas, V.,Kuranova, I.
Structure of the carboxypeptidase B complex with N-sulfamoyl-L-phenylalanine - a transition state analog of non-specific substrate.
J. Biomol. Struct. Dyn., 36:956-965, 2018

PubMed Abstract: Carboxypeptidase B (EC 3.4.17.2) (CPB) is commonly used in the industrial insulin production and as a template for drug design. However, its ability to discriminate substrates with hydrophobic, hydrophilic, and charged side chains is not well understood. We report structure of CPB complex with a transition state analog N-sulfamoyl-L-phenylalanine solved at 1.74Å. The study provided an insight into structural basis of CPB substrate specificity. Ligand binding is affected by structure-depended conformational changes of Asp255 in S1'-subsite, interactions with Asn144 and Arg145 in C-terminal binding subsite, and Glu270 in the catalytic center. Side chain of the non-specific substrate analog SPhe in comparison with that of specific substrate analog SArg (reported earlier) not only loses favorable electrostatic interactions and two hydrogen bonds with Asp255 and three fixed water molecules, but is forced to be in the unfavorable hydrophilic environment. Thus, Ser207, Gly253, Tyr248, and Asp255 residues play major role in the substrate recognition by S1'-subsite.

PubMed: 28274181
DOI: 10.1080/07391102.2017.1304242

実験手法

X-RAY DIFFRACTION (1.4 Å)