1HV6

CRYSTAL STRUCTURE OF ALGINATE LYASE A1-III COMPLEXED WITH TRISACCHARIDE PRODUCT.

1HV6 の概要

• エントリーDOI: 10.2210/pdb1hv6/pdb
• 関連するPDBエントリー: 1QAZ
• 分子名称: ALGINATE LYASE, 4-deoxy-alpha-L-erythro-hex-4-enopyranuronic acid-(1-4)-alpha-D-mannopyranuronic acid-(1-4)-alpha-D-glucopyranuronic acid, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: alginate lyase, trisaccharide complex, alpha barrel, lyase
• 由来する生物種: Sphingomonas sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40274.03

構造登録者

Yoon, H.-J.,Hashimoto, W.,Miyake, O.,Murata, K.,Mikami, B. (登録日: 2001-01-08, 公開日: 2001-05-02, 最終更新日: 2024-11-20)

主引用文献

Yoon, H.J.,Hashimoto, W.,Miyake, O.,Murata, K.,Mikami, B.
Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 A resolution.
J.Mol.Biol., 307:9-16, 2001

PubMed Abstract: The structure of A1-III from a Sphingomonas species A1 complexed with a trisaccharide product (4-deoxy-l-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid) was determined by X-ray crystallography at 2.0 A with an R-factor of 0.16. The final model of the complex form comprising 351 amino acid residues, 245 water molecules, one sulfate ion and one trisaccharide product exhibited a C(alpha) r.m.s.d. value of 0.154 A with the reported apo form of the enzyme. The trisaccharide was bound in the active cleft at subsites -3 approximately -1 from the non-reducing end by forming several hydrogen bonds and van der Waals interactions with protein atoms. The catalytic residue was estimated to be Tyr246, which existed between subsites -1 and +1 based on a mannuronic acid model oriented at subsite +1.

PubMed: 11243798
DOI: 10.1006/jmbi.2000.4509

実験手法

X-RAY DIFFRACTION (2 Å)