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PDBsum entry 1cxh
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Glycosyltransferase PDB id
1cxh

 

 

 

 

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Contents
Protein chain
686 a.a. *
Ligands
GLC-GLC-GLC-GLC
GLC-GLC ×3
Metals
_CA ×2
Waters ×195
* Residue conservation analysis
PDB id:
1cxh
Name: Glycosyltransferase
Title: Complex of cgtase with maltotetraose at room temperature and ph 9.6 based on diffraction data of a crystal soaked with maltoheptaose
Structure: Cyclodextrin glycosyltransferase. Chain: a. Synonym: cgtase. Ec: 2.4.1.19
Source: Bacillus circulans. Organism_taxid: 1397. Strain: 251
Resolution:
2.41Å     R-factor:   0.180     R-free:   0.200
Authors: R.M.A.Knegtel,B.V.Strokopytov,B.W.Dijkstra
Key ref: R.M.Knegtel et al. (1995). Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products. J Biol Chem, 270, 29256-29264. PubMed id: 7493956
Date:
31-Jul-95     Release date:   15-Dec-95    
PROCHECK
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 Headers
 References

Protein chain
P43379  (CDGT2_NIACI) -  Cyclomaltodextrin glucanotransferase from Niallia circulans
Seq:
Struc: 		 
Seq:
Struc: 		713 a.a.
686 a.a.
Key:    Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.4.1.19  - cyclomaltodextrin glucanotransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Degrades starch to cyclodextrins by formation of a 1,4-alpha-D- glucosidic bond.

 

 
J Biol Chem 270:29256-29264 (1995)
PubMed id: 7493956  
 
 
Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products.
R.M.Knegtel, B.Strokopytov, D.Penninga, O.G.Faber, H.J.Rozeboom, K.H.Kalk, L.Dijkhuizen, B.W.Dijkstra.
 
  ABSTRACT  
 
Asp-229, Glu-257, and Asp-328 constitute the catalytic residues in cyclodextrin glycosyl transferase from Bacillus circulans strain 251. Via site-directed mutagenesis constructed D229N, E257Q, and D328N mutant proteins showed a 4,000-60,000-fold reduction of cyclization activity. A D229N/E257Q double mutant showed a 700,000-fold reduction and was crystallized for use in soaking experiments with alpha-cyclodextrin. Crystal structures were determined of wild type CGTase soaked at elevated pH with alpha-cyclodextrin (resolution, 2.1 A) and maltoheptaose (2.4 A). In addition, structures at cryogenic temperature were solved of the unliganded enzyme (2.2 A) and of the D229N/E257Q mutant after soaking with alpha-cyclodextrin (2.6 A). In the crystals soaked in alpha-cyclodextrin and maltoheptaose, a maltotetraose molecule is observed to bind in the active site. Residue 229 is at hydrogen bonding distance from the C-6 hydroxyl group of the sugar, which after cleavage will contain the new reducing end. In the D229N/E257Q double mutant structure, two alpha-cyclodextrins are observed to replace two maltoses at the E-domain, thus providing structural information on product inhibition via binding to the enzyme's raw starch binding domain.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21084405 B.Cobucci-Ponzano, C.Zorzetti, A.Strazzulli, S.Carillo, E.Bedini, M.M.Corsaro, D.A.Comfort, R.M.Kelly, M.Rossi, and M.Moracci (2011).
A novel {alpha}-D-galactosynthase from Thermotoga maritima converts {beta}-D-galactopyranosyl azide to {alpha}-galacto-oligosaccharides.
  Glycobiology, 21, 448-456.  
19682075 C.Christiansen, M.Abou Hachem, S.Janecek, A.Viksø-Nielsen, A.Blennow, and B.Svensson (2009).
The carbohydrate-binding module family 20--diversity, structure, and function.
  FEBS J, 276, 5006-5029.  
18626642 Y.H.Liu, F.P.Lu, Y.Li, J.L.Wang, and C.Gao (2008).
Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations.
  Appl Microbiol Biotechnol, 80, 795-803.  
18157528 Y.H.Liu, F.P.Lu, Y.Li, X.B.Yin, Y.Wang, and C.Gao (2008).
Characterisation of mutagenised acid-resistant alpha-amylase expressed in Bacillus subtilis WB600.
  Appl Microbiol Biotechnol, 78, 85-94.  
17803687 S.Bozonnet, M.T.Jensen, M.M.Nielsen, N.Aghajari, M.H.Jensen, B.Kramhøft, M.Willemoës, S.Tranier, R.Haser, and B.Svensson (2007).
The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity.
  FEBS J, 274, 5055-5067.
PDB codes: 2qps 2qpu
16524921 S.A.van Hijum, S.Kralj, L.K.Ozimek, L.Dijkhuizen, and I.G.van Geel-Schutten (2006).
Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria.
  Microbiol Mol Biol Rev, 70, 157-176.  
16517633 Z.Wang, Q.Qi, and P.G.Wang (2006).
Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production.
  Appl Environ Microbiol, 72, 1873-1877.  
16216577 G.Polekhina, A.Gupta, B.J.van Denderen, S.C.Feil, B.E.Kemp, D.Stapleton, and M.W.Parker (2005).
Structural basis for glycogen recognition by AMP-activated protein kinase.
  Structure, 13, 1453-1462.
PDB codes: 1z0m 1z0n
15630515 Q.Qi, and W.Zimmermann (2005).
Cyclodextrin glucanotransferase: from gene to applications.
  Appl Microbiol Biotechnol, 66, 475-485.  
15939348 R.Rodríguez-Sanoja, N.Oviedo, and S.Sánchez (2005).
Microbial starch-binding domain.
  Curr Opin Microbiol, 8, 260-267.  
12554949 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.  
12930989 J.E.Nielsen, and J.A.McCammon (2003).
Calculating pKa values in enzyme active sites.
  Protein Sci, 12, 1894-1901.  
12930991 N.Pinotsis, D.D.Leonidas, E.D.Chrysina, N.G.Oikonomakos, and I.M.Mavridis (2003).
The binding of beta- and gamma-cyclodextrins to glycogen phosphorylase b: kinetic and crystallographic studies.
  Protein Sci, 12, 1914-1924.
PDB codes: 1p29 1p2b 1p2d 1p2g
12039719 D.Zhang, X.Li, and L.H.Zhang (2002).
Isomaltulose synthase from Klebsiella sp. strain LX3: gene cloning and characterization and engineering of thermostability.
  Appl Environ Microbiol, 68, 2676-2682.  
12220178 G.Parsiegla, A.Belaïch, J.P.Belaïch, and R.Haser (2002).
Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases.
  Biochemistry, 41, 11134-11142.
PDB codes: 1ia6 1ia7
11790748 N.Rashid, J.Cornista, S.Ezaki, T.Fukui, H.Atomi, and T.Imanaka (2002).
Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain.
  J Bacteriol, 184, 777-784.  
12200277 S.Kralj, G.H.van Geel-Schutten, H.Rahaoui, R.J.Leer, E.J.Faber, M.J.van der Maarel, and L.Dijkhuizen (2002).
Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha-(1-->4) and alpha-(1-->6) glucosidic bonds.
  Appl Environ Microbiol, 68, 4283-4291.  
11443082 M.Hemker, A.Stratmann, K.Goeke, W.Schröder, J.Lenz, W.Piepersberg, and H.Pape (2001).
Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50.
  J Bacteriol, 183, 4484-4492.  
11302176 T.Yokota, T.Tonozuka, S.Kamitori, and Y.Sakano (2001).
The deletion of amino-terminal domain in Thermoactinomyces vulgaris R-47 alpha-amylases: effects of domain N on activity, specificity, stability and dimerization.
  Biosci Biotechnol Biochem, 65, 401-408.  
11330677 T.Yokota, T.Tonozuka, Y.Shimura, K.Ichikawa, S.Kamitori, and Y.Sakano (2001).
Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
  Biosci Biotechnol Biochem, 65, 619-626.
PDB codes: 1jib 1jl8
11064053 A.D.Blackwood, and C.Bucke (2000).
Addition of polar organic solvents can improve the product selectivity of cyclodextrin glycosyltransferase. Solvent effects on cgtase.
  Enzyme Microb Technol, 27, 704-708.  
10651801 B.A.van der Veen, G.J.van Alebeek, J.C.Uitdehaag, B.W.Dijkstra, and L.Dijkhuizen (2000).
The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms.
  Eur J Biochem, 267, 658-665.  
10869182 J.C.Uitdehaag, G.J.van Alebeek, B.A.van Der Veen, L.Dijkhuizen, and B.W.Dijkstra (2000).
Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity.
  Biochemistry, 39, 7772-7780.
PDB codes: 1eo5 1eo7
11150610 J.E.Nielsen, and T.V.Borchert (2000).
Protein engineering of bacterial alpha-amylases.
  Biochim Biophys Acta, 1543, 253-274.  
10793202 L.M.Hamilton, C.T.Kelly, and W.M.Fogarty (2000).
Review: cyclodextrins and their interaction with amylolytic enzymes.
  Enzyme Microb Technol, 26, 561-567.  
10705452 N.Ichikawa, R.Fujisaka, and R.Kuribayashi (2000).
Requirement for lysine-19 of the yeast mitochondrial ATPase inhibitor for the stability of the inactivated inhibitor-F1Fo complex at higher pH.
  Biosci Biotechnol Biochem, 64, 89-95.  
10679895 N.Ishii, K.Haga, K.Yamane, and K.Harata (2000).
Crystal structure of asparagine 233-replaced cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011 determined at 1.9 A resolution.
  J Mol Recognit, 13, 35-43.
PDB code: 1d7f
10353816 B.Mikami, M.Adachi, T.Kage, E.Sarikaya, T.Nanmori, R.Shinke, and S.Utsumi (1999).
Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose.
  Biochemistry, 38, 7050-7061.
PDB codes: 1b90 1b9z
10872458 H.D.Ly, and S.G.Withers (1999).
Mutagenesis of glycosidases.
  Annu Rev Biochem, 68, 487-522.  
10491128 J.E.Nielsen, L.Beier, D.Otzen, T.V.Borchert, H.B.Frantzen, K.V.Andersen, and A.Svendsen (1999).
Electrostatics in the active site of an alpha-amylase.
  Eur J Biochem, 264, 816-824.  
9558324 A.K.Schmidt, S.Cottaz, H.Driguez, and G.E.Schulz (1998).
Structure of cyclodextrin glycosyltransferase complexed with a derivative of its main product beta-cyclodextrin.
  Biochemistry, 37, 5909-5915.
PDB code: 3cgt
9853672 K.Funane, N.Libessart, D.Stewart, T.Michishita, and J.Preiss (1998).
Analysis of essential histidine residues of maize branching enzymes by chemical modification and site-directed mutagenesis.
  J Protein Chem, 17, 579-590.  
9860832 R.Mosi, H.Sham, J.C.Uitdehaag, R.Ruiterkamp, B.W.Dijkstra, and S.G.Withers (1998).
Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase.
  Biochemistry, 37, 17192-17198.  
9195884 K.Sorimachi, M.F.Le Gal-Coëffet, G.Williamson, D.B.Archer, and M.P.Williamson (1997).
Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin.
  Structure, 5, 647-661.
PDB codes: 1ac0 1acz
9245426 R.Mosi, S.He, J.Uitdehaag, B.W.Dijkstra, and S.G.Withers (1997).
Trapping and characterization of the reaction intermediate in cyclodextrin glycosyltransferase by use of activated substrates and a mutant enzyme.
  Biochemistry, 36, 9927-9934.  
8672460 B.Strokopytov, R.M.Knegtel, D.Penninga, H.J.Rozeboom, K.H.Kalk, L.Dijkhuizen, and B.W.Dijkstra (1996).
Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity.
  Biochemistry, 35, 4241-4249.
PDB codes: 1dij 2dij
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. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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