1pj9
From Proteopedia
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|PDB= 1pj9 |SIZE=350|CAPTION= <scene name='initialview01'>1pj9</scene>, resolution 2.00Å | |PDB= 1pj9 |SIZE=350|CAPTION= <scene name='initialview01'>1pj9</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> |
- | + | |ACTIVITY= <span class='plainlinks'>[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] </span> | |
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1cdg|1CDG]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pj9 OCA], [http://www.ebi.ac.uk/pdbsum/1pj9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pj9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Dijkstra, B W.]] | [[Category: Dijkstra, B W.]] | ||
[[Category: Rozeboom, H J.]] | [[Category: Rozeboom, H J.]] | ||
- | [[Category: ACY]] | ||
- | [[Category: CA]] | ||
- | [[Category: GLC]] | ||
- | [[Category: MAL]] | ||
- | [[Category: MPD]] | ||
[[Category: cyclodextrin]] | [[Category: cyclodextrin]] | ||
[[Category: glycosyltransferase]] | [[Category: glycosyltransferase]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:00:23 2008'' |
Revision as of 20:00, 30 March 2008
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, resolution 2.00Å | |||||||
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Ligands: | , , , , | ||||||
Activity: | Cyclomaltodextrin glucanotransferase, with EC number 2.4.1.19 | ||||||
Related: | 1CDG
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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