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2dfz

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dfz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dfz OCA], [http://www.ebi.ac.uk/pdbsum/2dfz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2dfz RCSB]</span>
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'''Crystal structure of cyclodextrin-binding protein complexed with gamma-cyclodextrin'''
'''Crystal structure of cyclodextrin-binding protein complexed with gamma-cyclodextrin'''
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[[Category: Yamada, M.]]
[[Category: Yamada, M.]]
[[Category: Yoshida, H.]]
[[Category: Yoshida, H.]]
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[[Category: cyclodextrin]]
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[[Category: Cyclodextrin]]
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Revision as of 21:20, 3 May 2008

Template:STRUCTURE 2dfz

Crystal structure of cyclodextrin-binding protein complexed with gamma-cyclodextrin


Overview

The crystal structure of a Thermoactinomyces vulgaris cyclo/maltodextrin-binding protein (TvuCMBP) complexed with gamma-cyclodextrin has been determined. Like Escherichia coli maltodextrin-binding protein (EcoMBP) and other bacterial sugar-binding proteins, TvuCMBP consists of two domains, an N- and a C-domain, both of which are composed of a central beta-sheet surrounded by alpha-helices; the domains are joined by a hinge region containing three segments. gamma-Cyclodextrin is located at a cleft formed by the two domains. A common functional conformational change has been reported in this protein family, which involves switching from an open form to a sugar-transporter bindable form, designated a closed form. The TvuCMBP-gamma-cyclodextrin complex structurally resembles the closed form of EcoMBP, indicating that TvuCMBP complexed with gamma-cyclodextrin adopts the closed form. The fluorescence measurements also showed that the affinities of TvuCMBP for cyclodextrins were almost equal to those for maltooligosaccharides. Despite having similar folds, the sugar-binding site of the N-domain part of TvuCMBP and other bacterial sugar-binding proteins are strikingly different. In TvuCMBP, the side-chain of Leu59 protrudes from the N-domain part into the sugar-binding cleft and orients toward the central cavity of gamma-cyclodextrin, thus Leu59 appears to play the key role in binding. The cleft of the sugar-binding site of TvuCMBP is also wider than that of EcoMBP. These findings suggest that the sugar-binding site of the N-domain part and the wide cleft are critical in determining the specificity of TvuCMBP for gamma-cyclodextrin.

About this Structure

2DFZ is a Single protein structure of sequence from Thermoactinomyces vulgaris. Full crystallographic information is available from OCA.

Reference

Structural basis for cyclodextrin recognition by Thermoactinomyces vulgaris cyclo/maltodextrin-binding protein., Tonozuka T, Sogawa A, Yamada M, Matsumoto N, Yoshida H, Kamitori S, Ichikawa K, Mizuno M, Nishikawa A, Sakano Y, FEBS J. 2007 Apr;274(8):2109-20. Epub 2007 Mar 20. PMID:17371546 Page seeded by OCA on Sun May 4 00:20:52 2008

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