1OT2

Bacillus circulans strain 251 Cyclodextrin glycosyl transferase mutant D135N

Summary for 1OT2

• Entry DOI: 10.2210/pdb1ot2/pdb
• Related: 1cdg 1OT1
• Related PRD ID: PRD_900001
• Descriptor: Cyclomaltodextrin glucanotransferase, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, ... (10 entities in total)
• Functional Keywords: glycosyl transferase, cyclodextrin, transferase
• Biological source: Bacillus circulans
• Total number of polymer chains: 1
• Total formula weight: 78460.26

Authors

Rozeboom, H.J.,Dijkstra, B.W. (deposition date: 2003-03-21, release date: 2003-06-03, Last modification date: 2024-10-09)

Primary citation

Leemhuis, H.,Rozeboom, H.J.,Dijkstra, B.W.,Dijkhuizen, L.
The fully conserved Asp residue in Conserved sequence region I of the alpha-amylase Family is crucial for the Catalytic Site Architecture and Activity
Febs Lett., 541:47-51, 2003

PubMed Abstract: The alpha-amylase family is a large group of starch processing enzymes [Svensson, B. (1994) Plant Mol. Biol. 25, 141-157]. It is characterized by four short sequence motifs that contain the seven fully conserved amino acid residues in this family: two catalytic carboxylic acid residues and four substrate binding residues. The seventh conserved residue (Asp135) has no direct interactions with either substrates or products, but it is hydrogen-bonded to Arg227, which does bind the substrate in the catalytic site. Using cyclodextrin glycosyltransferase as an example, this paper provides for the first time definite biochemical and structural evidence that Asp135 is required for the proper conformation of several catalytic site residues and therefore for activity.

PubMed: 12706817
DOI: 10.1016/S0014-5793(03)00286-2

Experimental method

X-RAY DIFFRACTION (2.1 Å)