1v3k: Difference between revisions

Revision as of 07:33, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1v3k.png

Template:STRUCTURE 1v3k

Crystal structure of F283Y mutant cyclodextrin glycosyltransferaseCrystal structure of F283Y mutant cyclodextrin glycosyltransferase

Template:ABSTRACT PUBMED 14739329

About this StructureAbout this Structure

1V3K is a Single protein structure of sequence from Bacillus sp.. Full crystallographic information is available from OCA.

ReferenceReference

Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site., Kanai R, Haga K, Akiba T, Yamane K, Harata K, Protein Sci. 2004 Feb;13(2):457-65. PMID:14739329

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

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OCA

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-[[Image:1v3k.jpg|left|200px]]
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 {{STRUCTURE_1v3k|  PDB=1v3k  |  SCENE=  }}
-'''Crystal structure of F283Y mutant cyclodextrin glycosyltransferase'''
+===Crystal structure of F283Y mutant cyclodextrin glycosyltransferase===
-==Overview==
+<!--
-Cyclodextrin glycosyltransferase (CGTase) belonging to the alpha-amylase family mainly catalyzes transglycosylation and produces cyclodextrins from starch and related alpha-1,4-glucans. The catalytic site of CGTase specifically conserves four aromatic residues, Phe183, Tyr195, Phe259, and Phe283, which are not found in alpha-amylase. To elucidate the structural role of Phe283, we determined the crystal structures of native and acarbose-complexed mutant CGTases in which Phe283 was replaced with leucine (F283L) or tyrosine (F283Y). The temperature factors of the region 259-269 in native F283L increased &gt;10 A(2) compared with the wild type. The complex formation with acarbose not only increased the temperature factors (&gt;10 A(2)) but also changed the structure of the region 257-267. This region is stabilized by interactions of Phe283 with Phe259 and Leu260 and plays an important role in the cyclodextrin binding. The conformation of the side-chains of Glu257, Phe259, His327, and Asp328 in the catalytic site was altered by the mutation of Phe283 with leucine, and this indicates that Phe283 partly arranges the structure of the catalytic site through contacts with Glu257 and Phe259. The replacement of Phe283 with tyrosine decreased the enzymatic activity in the basic pH range. The hydroxyl group of Tyr283 forms hydrogen bonds with the carboxyl group of Glu257, and the pK(a) of Glu257 in F283Y may be lower than that in the wild type.
+The line below this paragraph, {{ABSTRACT_PUBMED_14739329}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14739329 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14739329}}
 ==About this Structure==
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 ==Reference==
 Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site., Kanai R, Haga K, Akiba T, Yamane K, Harata K, Protein Sci. 2004 Feb;13(2):457-65. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14739329 14739329]
+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:[http://www.ncbi.nlm.nih.gov/pubmed/14769878 14769878]
 [[Category: Bacillus sp.]]
 [[Category: Cyclomaltodextrin glucanotransferase]]
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 [[Category: Cgtase]]
 [[Category: Cyclodextrin]]
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