1ded: Difference between revisions
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New page: left|200px<br /><applet load="1ded" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ded, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ... |
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[[Image:1ded.gif|left|200px]]<br /><applet load="1ded" size=" | [[Image:1ded.gif|left|200px]]<br /><applet load="1ded" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ded, resolution 2.0Å" /> | caption="1ded, resolution 2.0Å" /> | ||
'''CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF ALKALOPHILIC ASPARAGINE 233-REPLACED CYCLODEXTRIN GLUCANOTRANSFERASE COMPLEXED WITH AN INHIBITOR, ACARBOSE, AT 2.0 A RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
The product specificity of cyclodextrin glucanotransferase (CGTase) from | 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. | ||
==About this Structure== | ==About this Structure== | ||
1DED is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with ACR and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cyclomaltodextrin_glucanotransferase Cyclomaltodextrin glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.19 2.4.1.19] Full crystallographic information is available from [http:// | 1DED is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_sp. Bacillus sp.] with <scene name='pdbligand=ACR:'>ACR</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cyclomaltodextrin_glucanotransferase Cyclomaltodextrin glucanotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.19 2.4.1.19] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DED OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 A resolution., Ishii N, Haga K, Yamane K, Harata K, J Biochem | Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 A resolution., Ishii N, Haga K, Yamane K, Harata K, J Biochem. 2000 Mar;127(3):383-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10731709 10731709] | ||
[[Category: Bacillus sp.]] | [[Category: Bacillus sp.]] | ||
[[Category: Cyclomaltodextrin glucanotransferase]] | [[Category: Cyclomaltodextrin glucanotransferase]] | ||
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[[Category: cyclodextrin glucanotransferase]] | [[Category: cyclodextrin glucanotransferase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:46 2008'' | ||
