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1btc
From Proteopedia
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(New page: 200px<br /><applet load="1btc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1btc, resolution 2.0Å" /> '''THREE-DIMENSIONAL STR...)
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Revision as of 09:47, 20 November 2007
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THREE-DIMENSIONAL STRUCTURE OF SOYBEAN BETA-AMYLASE DETERMINED AT 3.0 ANGSTROMS RESOLUTION: PRELIMINARY CHAIN TRACING OF THE COMPLEX WITH ALPHA-CYCLODEXTRIN
Overview
The three-dimensional structure of a complex of soybean beta-amylase [EC, 3.2.1.2] with an inhibitor, alpha-cyclodextrin, has been determined at 3.0, A resolution by X-ray diffraction analysis. Preliminary chain tracing, showed that the enzyme folded into large and small domains. The large, domain has a (beta alpha)8 super-secondary structure, while the smaller, one is formed from two long loops extending from the beta 3 and beta 4, strands of the (beta alpha)8 structure. The interface of the two domains, together with shorter loops from the (beta alpha)8 structure form a deep, cleft, in which alpha-cyclodextrin binds slightly away from the center., Two maltose molecules also bind in the cleft. One shares a binding site, with alpha-cyclodextrin and the other is situated more deeply in the, cleft.
About this Structure
1BTC is a Single protein structure of sequence from [1] with SO4 and BME as ligands. Active as Beta-amylase, with EC number 3.2.1.2 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of soybean beta-amylase determined at 3.0 A resolution: preliminary chain tracing of the complex with alpha-cyclodextrin., Mikami B, Sato M, Shibata T, Hirose M, Aibara S, Katsube Y, Morita Y, J Biochem (Tokyo). 1992 Oct;112(4):541-6. PMID:1491009
Page seeded by OCA on Tue Nov 20 11:54:23 2007
Categories: Beta-amylase | Single protein | Hehre, E.J. | Hirose, M. | Katsube, Y. | Mikami, B. | Morita, Y. | Sacchettini, J.C. | Sato, M. | BME | SO4 | Hydrolase(o-glycosyl)
