5NLT

CvAA9A

5NLT の概要

• エントリーDOI: 10.2210/pdb5nlt/pdb
• 分子名称: CvAA9A, COPPER (II) ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: enzyme, oxidoreductase
• 由来する生物種: Collariella virescens
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 167896.58

構造登録者

Frandsen, K.E.H.,Poulsen, J.-C.N.,Tandrup, T.,Schnorr, K.,Tovborg, M.,Lo Leggio, L. (登録日: 2017-04-04, 公開日: 2017-11-01, 最終更新日: 2024-01-17)

主引用文献

Simmons, T.J.,Frandsen, K.E.H.,Ciano, L.,Tryfona, T.,Lenfant, N.,Poulsen, J.C.,Wilson, L.F.L.,Tandrup, T.,Tovborg, M.,Schnorr, K.,Johansen, K.S.,Henrissat, B.,Walton, P.H.,Lo Leggio, L.,Dupree, P.
Structural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substrates.
Nat Commun, 8:1064-1064, 2017

PubMed Abstract: Lytic polysaccharide monooxygenases (LPMOs) are industrially important copper-dependent enzymes that oxidatively cleave polysaccharides. Here we present a functional and structural characterization of two closely related AA9-family LPMOs from Lentinus similis (LsAA9A) and Collariella virescens (CvAA9A). LsAA9A and CvAA9A cleave a range of polysaccharides, including cellulose, xyloglucan, mixed-linkage glucan and glucomannan. LsAA9A additionally cleaves isolated xylan substrates. The structures of CvAA9A and of LsAA9A bound to cellulosic and non-cellulosic oligosaccharides provide insight into the molecular determinants of their specificity. Spectroscopic measurements reveal differences in copper co-ordination upon the binding of xylan and glucans. LsAA9A activity is less sensitive to the reducing agent potential when cleaving xylan, suggesting that distinct catalytic mechanisms exist for xylan and glucan cleavage. Overall, these data show that AA9 LPMOs can display different apparent substrate specificities dependent upon both productive protein-carbohydrate interactions across a binding surface and also electronic considerations at the copper active site.

PubMed: 29057953
DOI: 10.1038/s41467-017-01247-3

実験手法

X-RAY DIFFRACTION (1.9 Å)