1TMQ

STRUCTURE OF TENEBRIO MOLITOR LARVAL ALPHA-AMYLASE IN COMPLEX WITH RAGI BIFUNCTIONAL INHIBITOR

Summary for 1TMQ

• Entry DOI: 10.2210/pdb1tmq/pdb
• Descriptor: PROTEIN (ALPHA-AMYLASE), PROTEIN (RAGI BIFUNCTIONAL INHIBITOR), CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: alpha-amylase, carbohydrate metabolism, alpha-1, 4-glucan-4-glucanohydrolase, hydrolase bifunctional alpha-amylase/trypsin inhibitor, complex (enzyme- inhibitor), hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Tenebrio molitor (yellow mealworm); More
• Total number of polymer chains: 2
• Total formula weight: 64054.42

Authors

Gomis-Rueth, F.X.,Strobl, S.,Glockshuber, R. (deposition date: 1998-01-13, release date: 1999-03-02, Last modification date: 2024-11-13)

Primary citation

Strobl, S.,Maskos, K.,Wiegand, G.,Huber, R.,Gomis-Ruth, F.X.,Glockshuber, R.
A novel strategy for inhibition of alpha-amylases: yellow meal worm alpha-amylase in complex with the Ragi bifunctional inhibitor at 2.5 A resolution.
Structure, 6:911-921, 1998

PubMed Abstract: alpha-Amylases catalyze the hydrolysis of alpha-D-(1,4)-glucan linkages in starch and related compounds. There is a wide range of industrial and medical applications for these enzymes and their inhibitors. The Ragi bifunctional alpha-amylase/trypsin inhibitor (RBI) is the prototype of the cereal inhibitor superfamily and is the only member of this family that inhibits both trypsin and alpha-amylases. The mode of inhibition of alpha-amylases by these cereal inhibitors has so far been unknown.

PubMed: 9687373
DOI: 10.1016/S0969-2126(98)00092-6

Experimental method

X-RAY DIFFRACTION (2.5 Å)