1OJM

SPECIFICITY AND MECHANISM OF STREPTOCOCCUS PNEUMONIAE HYALURONATE LYASE: COMPLEX WITH UNSULPHATED CHONDROITIN DISACCHARIDE

1OJM の概要

• エントリーDOI: 10.2210/pdb1ojm/pdb
• 関連するPDBエントリー: 1C82 1EGU 1F9G 1LOH 1LXK 1N7N 1N7O 1N7P 1N7Q 1N7R 1OJN 1OJO 1OJP
• 関連するBIRD辞書のPRD_ID: PRD_900058
• 分子名称: HYALURONATE LYASE, 4-deoxy-alpha-L-threo-hex-4-enopyranuronic acid-(1-3)-2-acetamido-2-deoxy-beta-D-galactopyranose, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: lyase, protein-carbohydrate complex
• 由来する生物種: STREPTOCOCCUS PNEUMONIAE
• 細胞内の位置: Secreted, cell wall; Peptidoglycan-anchor (Potential): Q54873
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 84167.35

構造登録者

Rigden, D.J.,Jedrzejas, M.J. (登録日: 2003-07-11, 公開日: 2003-10-30, 最終更新日: 2023-12-13)

主引用文献

Rigden, D.J.,Jedrzejas, M.J.
Structures of Streptococcus Pneumoniae Hyaluronate Lyase in Complex with Chondroitin and Chondroitin Sulfate Disaccharides: Insights Into Specificity and Mechanism of Action
J.Biol.Chem., 278:50596-, 2003

PubMed Abstract: Streptococcus pneumoniae hyaluronate lyase is a surface enzyme of this Gram-positive bacterium. The enzyme degrades hyaluronan and chondroitin/chondroitin sulfates by cleaving the beta1,4-glycosidic linkage between the glycan units of these polymeric substrates. This degradation helps spreading of this bacterial organism throughout the host tissues and facilitates the disease process caused by pneumococci. The mechanism of this degradative process is based on beta-elimination, is termed proton acceptance and donation, and involves selected residues of a well defined catalytic site of the enzyme. The degradation of hyaluronan alone is thought to proceed through a processive mode of action. The structures of complexes between the enzyme and chondroitin as well as chondroitin sulfate disaccharides allowed for the first detailed insights into these interactions and the mechanism of action on chondroitins. This degradation of chondroitin/chondroitin sulfates is nonprocessive and is selective for the chondroitin sulfates only with certain sulfation patterns. Chondroitin sulfation at the 4-position on the nonreducing site of the linkage to be cleaved or 2-sulfation prevent degradation due to steric clashes with the enzyme. Evolutionary studies suggest that hyaluronate lyases evolved from chondroitin lyases and still retained chondroitin/chondroitin sulfate degradation abilities while being specialized in the degradation of hyaluronan. The more efficient processive degradation mechanism has come to be preferred for the unsulfated substrate hyaluronan.

PubMed: 14523022
DOI: 10.1074/JBC.M307596200

実験手法

X-RAY DIFFRACTION (1.78 Å)