4AEE

CRYSTAL STRUCTURE OF MALTOGENIC AMYLASE FROM S.MARINUS

Summary for 4AEE

• Entry DOI: 10.2210/pdb4aee/pdb
• Descriptor: ALPHA AMYLASE, CATALYTIC REGION (2 entities in total)
• Functional Keywords: hydrolase, hyperthermostable, cyclodextrin hydrolase, gh13
• Biological source: STAPHYLOTHERMUS MARINUS
• Total number of polymer chains: 2
• Total formula weight: 165151.50

Authors

Jung, T.Y.,Park, C.H.,Yoon, S.M.,Park, S.H.,Park, K.H.,Woo, E.J. (deposition date: 2012-01-10, release date: 2012-01-18, Last modification date: 2012-03-21)

Primary citation

Jung, T.Y.,Li, D.,Park, J.T.,Yoon, S.M.,Tran, P.L.,Oh, B.H.,Janecek, S.,Park, S.G.,Woo, E.J.,Park, K.H.
Association of Novel Domain in Active Site of Archaic Hyperthermophilic Maltogenic Amylase from Staphylothermus Marinus.
J.Biol.Chem., 287:7979-, 2012

PubMed Abstract: Staphylothermus marinus maltogenic amylase (SMMA) is a novel extreme thermophile maltogenic amylase with an optimal temperature of 100 °C, which hydrolyzes α-(1-4)-glycosyl linkages in cyclodextrins and in linear malto-oligosaccharides. This enzyme has a long N-terminal extension that is conserved among archaic hyperthermophilic amylases but is not found in other hydrolyzing enzymes from the glycoside hydrolase 13 family. The SMMA crystal structure revealed that the N-terminal extension forms an N' domain that is similar to carbohydrate-binding module 48, with the strand-loop-strand region forming a part of the substrate binding pocket with several aromatic residues, including Phe-95, Phe-96, and Tyr-99. A structural comparison with conventional cyclodextrin-hydrolyzing enzymes revealed a striking resemblance between the SMMA N' domain position and the dimeric N domain position in bacterial enzymes. This result suggests that extremophilic archaea that live at high temperatures may have adopted a novel domain arrangement that combines all of the substrate binding components within a monomeric subunit. The SMMA structure provides a molecular basis for the functional properties that are unique to hyperthermophile maltogenic amylases from archaea and that distinguish SMMA from moderate thermophilic or mesophilic bacterial enzymes.

PubMed: 22223643
DOI: 10.1074/JBC.M111.304774

Experimental method

X-RAY DIFFRACTION (2.28 Å)