5H05

Crystal structure of AmyP E221Q in complex with MALTOTRIOSE

Summary for 5H05

• Entry DOI: 10.2210/pdb5h05/pdb
• Related: 5H06
• Related PRD ID: PRD_900009
• Descriptor: AmyP, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: alpha-amylase, gh13_37, hydrolase
• Biological source: marine metagenome
• Total number of polymer chains: 4
• Total formula weight: 284442.60

Authors

He, C.,Liu, Y. (deposition date: 2016-10-03, release date: 2017-08-16, Last modification date: 2024-10-16)

Primary citation

Liu, Y.,Yu, J.,Li, F.,Peng, H.,Zhang, X.,Xiao, Y.,He, C.
Crystal structure of a raw-starch-degrading bacterial alpha-amylase belonging to subfamily 37 of the glycoside hydrolase family GH13
Sci Rep, 7:44067-44067, 2017

PubMed Abstract: Subfamily 37 of the glycoside hydrolase family GH13 was recently established on the basis of the discovery of a novel α-amylase, designated AmyP, from a marine metagenomic library. AmyP exhibits raw-starch-degrading activity and consists of an N-terminal catalytic domain and a C-terminal starch-binding domain. To understand this newest subfamily, we determined the crystal structure of the catalytic domain of AmyP, named AmyP, complexed with maltose, and the crystal structure of the E221Q mutant AmyP complexed with maltotriose. Glu221 is one of the three conserved catalytic residues, and AmyP is inactivated by the E221Q mutation. Domain B of AmyP forms a loop that protrudes from domain A, stabilizes the conformation of the active site and increases the thermostability of the enzyme. A new calcium ion is situated adjacent to the -3 subsite binding loop and may be responsible for the increased thermostability of the enzyme after the addition of calcium. Moreover, Tyr36 participates in both stacking and hydrogen bonding interactions with the sugar motif at subsite -3. This work provides the first insights into the structure of α-amylases belonging to subfamily 37 of GH13 and may contribute to the rational design of α-amylase mutants with enhanced performance in biotechnological applications.

PubMed: 28303907
DOI: 10.1038/srep44067

Experimental method

X-RAY DIFFRACTION (2.55 Å)