1pj9

From Proteopedia

Bacillus circulans strain 251 loop mutant 183-195

Structural highlights

1pj9 is a 1 chain structure with sequence from Niallia circulans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CDGT2_NIACI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Leemhuis H, Rozeboom HJ, Dijkstra BW, Dijkhuizen L. Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge. Proteins. 2004 Jan 1;54(1):128-34. PMID:14705029 doi:10.1002/prot.10516