5XQ3

Crystal structure of a PL 26 exo-rhamnogalacturonan lyase from Penicillium chrysogenum

5XQ3 の概要

• エントリーDOI: 10.2210/pdb5xq3/pdb
• 分子名称: Pcrglx protein, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: exo-rhamnogalacturonan lyase, enzyme, pectin, sad, se, lyase
• 由来する生物種: Penicillium chrysogenum; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 201967.40

構造登録者

Kunishige, Y.,Iwai, M.,Tada, T.,Nishimura, S.,Sakamoto, T. (登録日: 2017-06-06, 公開日: 2018-03-21, 最終更新日: 2024-11-06)

主引用文献

Kunishige, Y.,Iwai, M.,Nakazawa, M.,Ueda, M.,Tada, T.,Nishimura, S.,Sakamoto, T.
Crystal structure of exo-rhamnogalacturonan lyase from Penicillium chrysogenum as a member of polysaccharide lyase family 26
FEBS Lett., 592:1378-1388, 2018

PubMed Abstract: Exo-rhamnogalacturonan lyase from Penicillium chrysogenum 31B (PcRGLX) was recently classified as a member of polysaccharide lyase (PL) family 26 along with hypothetical proteins derived from various organisms. In this study, we determined the crystal structure of PcRGLX as the first structure of a member of this family. Based on the substrate-binding orientation and substrate specificity, PcRGLX is an exo-type PL that cleaves rhamnogalacturonan from the reducing end. Analysis of PcRGLX-complex structures with reaction products indicate that the active site possesses an L-shaped cleft that can accommodate galactosyl side chains, suggesting side-chain-bypassing activity in PcRGLX. Furthermore, we determined the residues critical for catalysis by analyzing the enzyme activities of inactive variants.

PubMed: 29574769
DOI: 10.1002/1873-3468.13034

実験手法

X-RAY DIFFRACTION (2.85 Å)