1pj9

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(New page: 200px<br /><applet load="1pj9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pj9, resolution 2.00&Aring;" /> '''Bacillus circulans s...)
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caption="1pj9, resolution 2.00&Aring;" />
'''Bacillus circulans strain 251 loop mutant 183-195'''<br />
'''Bacillus circulans strain 251 loop mutant 183-195'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1PJ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans] with MAL, GLC, CA, MPD and ACY 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PJ9 OCA].
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1PJ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_circulans Bacillus circulans] with <scene name='pdbligand=MAL:'>MAL</scene>, <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=MPD:'>MPD</scene> and <scene name='pdbligand=ACY:'>ACY</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=1PJ9 OCA].
==Reference==
==Reference==
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[[Category: Cyclomaltodextrin glucanotransferase]]
[[Category: Cyclomaltodextrin glucanotransferase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dijkstra, B.W.]]
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[[Category: Dijkstra, B W.]]
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[[Category: Rozeboom, H.J.]]
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[[Category: Rozeboom, H J.]]
[[Category: ACY]]
[[Category: ACY]]
[[Category: CA]]
[[Category: CA]]
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:51:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:29:20 2008''

Revision as of 12:29, 21 February 2008


1pj9, resolution 2.00Å

Drag the structure with the mouse to rotate

Bacillus circulans strain 251 loop mutant 183-195

Overview

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.

About this Structure

1PJ9 is a Single protein structure of sequence from Bacillus circulans with , , , and as ligands. Active as Cyclomaltodextrin glucanotransferase, with EC number 2.4.1.19 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

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