1JL8

Complex of alpha-amylase II (TVA II) from Thermoactinomyces vulgaris R-47 with beta-cyclodextrin based on a co-crystallization with methyl beta-cyclodextrin

Summary for 1JL8

• Entry DOI: 10.2210/pdb1jl8/pdb
• Related: 1BVZ 1G1Y 1JIB
• Related PRD ID: PRD_900012
• Descriptor: ALPHA-AMYLASE II, Cycloheptakis-(1-4)-(alpha-D-glucopyranose) (2 entities in total)
• Functional Keywords: pullulan, cyclodextrin, neopullulanase, methyl beta-cyclodextrin, beta-cyclodextrin, hydrolase
• Biological source: Thermoactinomyces vulgaris
• Total number of polymer chains: 2
• Total formula weight: 137412.25

Authors

Yokota, T.,Tonozuka, T.,Shimura, Y.,Ichikawa, K.,Kamitori, S.,Sakano, Y. (deposition date: 2001-07-16, release date: 2001-08-01, Last modification date: 2023-10-25)

Primary citation

Yokota, T.,Tonozuka, T.,Shimura, Y.,Ichikawa, K.,Kamitori, S.,Sakano, Y.
Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
Biosci.Biotechnol.Biochem., 65:619-626, 2001

PubMed Abstract: The structures of Thermoactinomyces vulgaris R-47 alpha-amylase II mutant (d325nTVA II) complexed with substrate analogues, methyl beta-cyclodextrin (m beta-CD) and maltohexaose (G6), were solved by X-ray diffraction at 3.2 A and 3.3 A resolution, respectively. In d325nTVA II-m beta-CD complex, the orientation and binding-position of beta-CD in TVA II were identical to those in cyclodextin glucanotransferase (CGTase). The active site residues were essentialy conserved, while there are no residues corresponding to Tyr89, Phe183, and His233 of CGTase in TVA II. In d325nTVA II-G6 complex, the electron density maps of two glucosyl units at the non-reducing end were disordered and invisible. The four glucosyl units of G6 were bound to TVA II as in CGTase, while the others were not stacked and were probably flexible. The residues of TVA II corresponding to Tyr89, Lys232, and His233 of CGTase were completely lacking. These results suggest that the lack of the residues related to alpha-glucan and CD-stacking causes the functional distinctions between CGTase and TVA II.

PubMed: 11330677
DOI: 10.1271/bbb.65.619

Experimental method

X-RAY DIFFRACTION (3.2 Å)