 |
PDBsum entry 1ded
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Transferase
|
|
|
Title:
|
|
Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 a resolution
|
|
Structure:
|
|
Cyclodextrin glucanotransferase. Chain: a, b. Fragment: cyclodextrin glucanotransferase (cgtase). Synonym: cgtase. Engineered: yes. Mutation: yes
|
|
Source:
|
|
Bacillus sp.. Organism_taxid: 1410. Strain: 1011. Expressed in: escherichia coli. Expression_system_taxid: 562.
|
|
Resolution:
|
|
|
2.00Å
|
R-factor:
|
0.163
|
R-free:
|
0.222
|
|
|
Authors:
|
|
N.Ishii,K.Haga,K.Yamane,K.Harata
|
|
Key ref:
|
|
N.Ishii
et al.
(2000).
Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 A resolution.
J Biochem (tokyo),
127,
383-391.
PubMed id:
|
|
|
Date:
|
|
|
14-Nov-99
|
Release date:
|
07-Apr-00
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P05618
(CDGT_BACS0) -
Cyclomaltodextrin glucanotransferase from Bacillus sp. (strain 1011)
|
|
|
|
Seq:
Struc:
|
|
|
|
713 a.a.
686 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Key: |
|
 |
Secondary structure |
|
 |
CATH domain |
|
|
*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.2.4.1.19
- cyclomaltodextrin glucanotransferase.
|
|
|
|
|
|
|
Reaction:
|
|
Degrades starch to cyclodextrins by formation of a 1,4-alpha-D- glucosidic bond.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
J Biochem (tokyo)
127:383-391
(2000)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Crystal structure of alkalophilic asparagine 233-replaced cyclodextrin glucanotransferase complexed with an inhibitor, acarbose, at 2.0 A resolution.
|
|
N.Ishii,
K.Haga,
K.Yamane,
K.Harata.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
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.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
J.Y.Damián-Almazo,
A.Moreno,
A.López-Munguía,
X.Soberón,
F.González-Muñoz,
and
G.Saab-Rincón
(2008).
Enhancement of the alcoholytic activity of alpha-amylase AmyA from Thermotoga maritima MSB8 (DSM 3109) by site-directed mutagenesis.
|
| |
Appl Environ Microbiol,
74,
5168-5177.
|
|
|
|
|
|
|
H.W.Choe,
K.S.Park,
J.Labahn,
J.Granzin,
C.J.Kim,
and
G.Büldt
(2003).
Crystallization and preliminary X-ray diffraction studies of alpha-cyclodextrin glucanotransferase isolated from Bacillus macerans.
|
| |
Acta Crystallogr D Biol Crystallogr,
59,
348-349.
|
|
|
|
|
|
|
E.A.MacGregor,
S.Janecek,
and
B.Svensson
(2001).
Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
|
| |
Biochim Biophys Acta,
1546,
1.
|
|
|
|
|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
|
|
Links
