7EAP

Crystal structure of IpeA-XXXG complex

Summary for 7EAP

• Entry DOI: 10.2210/pdb7eap/pdb
• Descriptor: Fn3_like domain-containing protein, alpha-D-xylopyranose-(1-6)-beta-D-glucopyranose-(1-4)-[alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-[alpha-D-xylopyranose-(1-6)]beta-D-glucopyranose-(1-4)-beta-D-glucopyranose, alpha-D-xylopyranose-(1-6)-beta-D-glucopyranose, ... (7 entities in total)
• Functional Keywords: glycoside hydrolase family 3, isoprimeverose-producing oligoxyloglucan hydrolase, xyloglucan oligosaccharides, hydrolase
• Biological source: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
• Total number of polymer chains: 1
• Total formula weight: 87196.23

Authors

Matsuzawa, T.,Watanabe, M.,Nakamichi, Y.,Akita, H.,Yaoi, K. (deposition date: 2021-03-08, release date: 2022-03-16, Last modification date: 2024-11-06)

Primary citation

Matsuzawa, T.,Watanabe, M.,Nakamichi, Y.,Akita, H.,Yaoi, K.
Structural basis for the catalytic mechanism of the glycoside hydrolase family 3 isoprimeverose-producing oligoxyloglucan hydrolase from Aspergillus oryzae.
Febs Lett., 596:1944-1954, 2022

PubMed Abstract: Aspergillus oryzae isoprimeverose-producing oligoxyloglucan hydrolase (IpeA) releases isoprimeverose units (α-d-xylopyranosyl-(1→6)-d-glucose) from the non-reducing end of xyloglucan oligosaccharides and belongs to glycoside hydrolase family 3. In this paper, we report the X-ray crystal structure of the IpeA complexed with a xyloglucan oligosaccharide, (XXXG: Glc Xyl ). Trp515 of IpeA plays a critical role in XXXG recognition at positive subsites. In addition, docking simulation of IpeA-XXXG suggested that two Tyr residues (Tyr268 and Tyr445) are involved in the catalytic reaction mechanism of IpeA. Tyr268 plays an important role in product turnover, whereas Tyr445 stabilizes the acid/base Glu524 residue, which serves as a proton donor. Our findings indicate that the substrate recognition machinery of IpeA is specifically adapted to xyloglucan oligosaccharides.

PubMed: 35717558
DOI: 10.1002/1873-3468.14427

Experimental method

X-RAY DIFFRACTION (1.42 Å)