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1pj9

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[[Image:1pj9.jpg|left|200px]]
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{{STRUCTURE_1pj9| PDB=1pj9 | SCENE= }}
{{STRUCTURE_1pj9| PDB=1pj9 | SCENE= }}
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'''Bacillus circulans strain 251 loop mutant 183-195'''
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===Bacillus circulans strain 251 loop mutant 183-195===
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==Overview==
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Cyclodextrin glycosyltransferase (CGTase) catalyzes the formation of cyclodextrins from starch. Among the CGTases with known three-dimensional structure, Thermoanaerobacterium thermosulfurigenes CGTase has the highest thermostability. By replacing amino acid residues in the B-domain of Bacillus circulans CGTase with those from T. thermosulfurigenes CGTase, we identified a B. circulans CGTase mutant (with N188D and K192R mutations), with a strongly increased activity half-life at 60 degrees C. Asp188 and Arg192 form a salt bridge in T. thermosulfurigenes CGTase. Structural analysis of the B. circulans CGTase mutant revealed that this salt bridge is also formed in the mutant. Thus, the activity half-life of this enzyme can be enhanced by rational protein engineering.
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(as it appears on PubMed at http://www.pubmed.gov), where 14705029 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14705029}}
==About this Structure==
==About this Structure==
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[[Category: Glycosyltransferase]]
[[Category: Glycosyltransferase]]
[[Category: Transferase]]
[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:08:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:53:53 2008''

Revision as of 12:53, 28 July 2008

Image:1pj9.png

Template:STRUCTURE 1pj9

Bacillus circulans strain 251 loop mutant 183-195

Template:ABSTRACT PUBMED 14705029

About this Structure

1PJ9 is a Single protein structure of sequence from Bacillus circulans. Full crystallographic information is available from OCA.

Reference

Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge., Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L, Proteins. 2004 Jan 1;54(1):128-34. PMID:14705029

Page seeded by OCA on Mon Jul 28 15:53:53 2008

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