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1uks

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[[Image:1uks.gif|left|200px]]
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{{STRUCTURE_1uks| PDB=1uks | SCENE= }}
{{STRUCTURE_1uks| PDB=1uks | SCENE= }}
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'''Crystal structure of F183L/F259L mutant cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose'''
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===Crystal structure of F183L/F259L mutant cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose===
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==Overview==
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The stacking interaction between a tyrosine residue and the sugar ring at the catalytic subsite -1 is strictly conserved in the glycoside hydrolase family 13 enzymes. Replacing Tyr100 with leucine in cyclodextrin glycosyltransferase (CGTase) from Bacillus sp. 1011 to prevent stacking significantly decreased all CGTase activities. The adjacent stacking interaction with both Phe183 and Phe259 onto the sugar ring at subsite +2 is essentially conserved among CGTases. F183L/F259L mutant CGTase affects donor substrate binding and/or acceptor binding during transglycosylation [Nakamura et al. (1994) Biochemistry 33, 9929-9936]. To elucidate the precise role of carbohydrate/aromatic stacking interaction at subsites -1 and +2 on the substrate binding of CGTases, we analyzed the X-ray structures of wild-type (2.0 A resolution), and Y100L (2.2 A resolution) and F183L/F259L mutant (1.9 A resolution) CGTases complexed with the inhibitor, acarbose. The refined structures revealed that acarbose molecules bound to the Y100L mutant moved from the active center toward the side chain of Tyr195, and the hydrogen bonding and hydrophobic interaction between acarbose and subsites significantly diminished. The position of pseudo-tetrasaccharide binding in the F183L/F259L mutant was closer to the non-reducing end, and the torsion angles of glycosidic linkages at subsites -1 to +1 on molecule 1 and subsites -2 to -1 on molecule 2 significantly changed compared with that of each molecule of wild-type-acarbose complex to adopt the structural change of subsite +2. These structural and biochemical data suggest that substrate binding in the active site of CGTase is critically affected by the carbohydrate/aromatic stacking interaction with Tyr100 at the catalytic subsite -1 and that this effect is likely a result of cooperation between Tyr100 and Phe259 through stacking interaction with substrate at subsite +2.
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(as it appears on PubMed at http://www.pubmed.gov), where 14769878 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14769878}}
==About this Structure==
==About this Structure==
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[[Category: Carbohydrate/protein interaction]]
[[Category: Carbohydrate/protein interaction]]
[[Category: Cgtase]]
[[Category: Cgtase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:21:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:28:33 2008''

Revision as of 09:28, 29 July 2008

Image:1uks.png

Template:STRUCTURE 1uks

Crystal structure of F183L/F259L mutant cyclodextrin glucanotransferase complexed with a pseudo-maltotetraose derived from acarbose

Template:ABSTRACT PUBMED 14769878

About this Structure

1UKS is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.

Reference

Effects of essential carbohydrate/aromatic stacking interaction with Tyr100 and Phe259 on substrate binding of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp. 1011., Haga K, Kanai R, Sakamoto O, Aoyagi M, Harata K, Yamane K, J Biochem. 2003 Dec;134(6):881-91. PMID:14769878

Page seeded by OCA on Tue Jul 29 12:28:33 2008

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