3NIP

Crystal structure of Pseudomonas aeruginosa guanidinopropionase complexed with 1,6-diaminohexane

3NIP の概要

• エントリーDOI: 10.2210/pdb3nip/pdb
• 関連するPDBエントリー: 3NIO 3NIQ
• 分子名称: 3-guanidinopropionase, HEXANE-1,6-DIAMINE (3 entities in total)
• 機能のキーワード: guanidinopropionase, gpua, pa0288, hydrolase
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 212368.69

構造登録者

Lee, S.J.,Kim, H.S.,Kim, D.J.,Yoon, H.J.,Kim, K.H.,Yoon, J.Y.,Jang, J.Y.,Im, H.,An, D.,Suh, S.W. (登録日: 2010-06-16, 公開日: 2011-06-01, 最終更新日: 2023-11-01)

主引用文献

Lee, S.J.,Kim, D.J.,Kim, H.S.,Lee, B.I.,Yoon, H.J.,Yoon, J.Y.,Kim, K.H.,Jang, J.Y.,Im, H.N.,An, D.R.,Song, J.S.,Kim, H.J.,Suh, S.W.
Crystal structures of Pseudomonas aeruginosa guanidinobutyrase and guanidinopropionase, members of the ureohydrolase superfamily
J.Struct.Biol., 175:329-338, 2011

PubMed Abstract: Pseudomonas aeruginosa guanidinobutyrase (GbuA) and guanidinopropionase (GpuA) catalyze the hydrolysis of 4-guanidinobutyrate and 3-guanidinopropionate, respectively. They belong to the ureohydrolase superfamily, which includes arginase, agmatinase, proclavaminate amidinohydrolase, and formiminoglutamase. In this study, we have determined the crystal structures of GbuA and GpuA from P. aeruginosa to provide a structural insight into their substrate specificity. Although GbuA and GpuA share a common structural fold of the typical ureohydrolase superfamily, they exhibit significant variations in two active site loops. Mutagenesis of Met161 of GbuA and Tyr157 of GpuA, both of which are located in the active site loop 1 and predicted to be involved in substrate recognition, significantly affected their enzymatic properties, implying their important roles in catalysis.

PubMed: 21600989
DOI: 10.1016/j.jsb.2011.05.002

実験手法

X-RAY DIFFRACTION (2.5 Å)