1ded: Difference between revisions

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~~'''~~CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION~~'''~~

===CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION===

~~==Overview==~~

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The product specificity of cyclodextrin glucanotransferase (CGTase) from alkalophilic Bacillus sp. #1011 is improved to near-uniformity by mutation of histidine-233 to asparagine. Asparagine 233-replaced CGTase (H233N-CGTase) no longer produces alpha-cyclodextrin, ~~while the wild-type CGTase from the same bacterium produces a mixture of predominantly alpha-~~, ~~beta-, and gamma-cyclodextrins, catalyzing~~ the ~~conversion of starch into cyclic or linear alpha-1,4-linked glucopyranosyl chains. In order~~ to ~~better understand~~ the ~~protein engineering of H233N-CGTase, the crystal structure of the mutant enzyme complexed with a maltotetraose analog, acarbose, was determined~~ at 2.~~0 A resolution with a final crystallographic R value of 0~~.~~163 for all data. Taking a close look at the active site cleft in which the acarbose molecule~~ is ~~bound,~~ the ~~most probable reason for the improved specificity of H233N~~-~~CGTase is the removal of interactions needed to form a compact ring like a~~-~~cyclodextrin.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10731709}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10731709 is the PubMed ID number.

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==About this Structure==

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[[Category: Cgtase]]

[[Category: Cyclodextrin glucanotransferase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:45:32 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:54:07 2008''

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-[[Image:1ded.gif|left|200px]]
+{{Seed}}
+[[Image:1ded.png|left|200px]]
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 {{STRUCTURE_1ded|  PDB=1ded  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION'''
+===CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION===
-==Overview==
+<!--
-The product specificity of cyclodextrin glucanotransferase (CGTase) from alkalophilic Bacillus sp. #1011 is improved to near-uniformity by mutation of histidine-233 to asparagine. Asparagine 233-replaced CGTase (H233N-CGTase) no longer produces alpha-cyclodextrin, while the wild-type CGTase from the same bacterium produces a mixture of predominantly alpha-, beta-, and gamma-cyclodextrins, catalyzing the conversion of starch into cyclic or linear alpha-1,4-linked glucopyranosyl chains. In order to better understand the protein engineering of H233N-CGTase, the crystal structure of the mutant enzyme complexed with a maltotetraose analog, acarbose, was determined at 2.0 A resolution with a final crystallographic R value of 0.163 for all data. Taking a close look at the active site cleft in which the acarbose molecule is bound, the most probable reason for the improved specificity of H233N-CGTase is the removal of interactions needed to form a compact ring like a-cyclodextrin.
+The line below this paragraph, {{ABSTRACT_PUBMED_10731709}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10731709 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10731709}}
 ==About this Structure==
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 [[Category: Cgtase]]
 [[Category: Cyclodextrin glucanotransferase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:45:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:54:07 2008''