Crystal structure of <i>Bacillus licheniformis</i> 1,3‐1,4‐β‐<scp>d</scp>‐glucan 4‐glucanohydrolase at 1.8 Å resolution

Hahn, Michael G.; Pons, Jaume; Planas, Antoni; Querol, Enrique; Heinemann, Udo

doi:10.1016/0014-5793(95)01111-q

Cited by 78 publications

(61 citation statements)

References 27 publications

(26 reference statements)

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“…The molecules have a slightly elongated shape with a prominent cleft crossing one side. This cleft originates from the twist and bending of the two ␤-sheets, arranged on top of each other in a sandwich-like manner, and from the loop regions as already described for lichenase (37). The cleft is at least 35 Å long for both ␤-AgaA_CM and ␤-AgaB and is equally lined with aromatic residues, listed in Table II.…”

Section: Resultsmentioning

confidence: 73%

“…In ␤-AgaB, a calcium ion is located at the same position but coordinated in a pentahedral manner to the backbone carbonyl oxygen atom of Asn-83, Gly-127, and Asp-343, a carboxylate oxygen of Asp-343, and one water molecule. It is interesting to note that this structural calcium ion is also found in the other GH-16 members with known three-dimensional structures (lichenases and -carrageenase) (24,37) and that the aspartic acid responsible for the only side-chain interaction with calcium is conserved (Fig. 4).…”

Section: Structural Comparison With Family Gh-16 Enzymes-mentioning

confidence: 78%

“…The sandwich fold of ␤-AgaA_CM and ␤-AgaB has the same number of ␤-strands as in -carrageenase (24) and in ␤-1,3- 1,4-glucanases (37). However, some extra structural elements are found in the loops connecting the internal and external strands of the two ␤-sheets.…”

Section: Structural Comparison With Family Gh-16 Enzymes-mentioning

confidence: 96%

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The Three-dimensional Structures of Two β-Agarases

Allouch

Jam

Helbert

et al. 2003

Journal of Biological Chemistry

129

132

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Agars are important gelifying agents for biochemical use and the food industry. To cleave the ␤-1,4-linkages between ␤-D-galactose and ␣-L-3,6-anhydro-galactose residues in the red algal galactans known as agars, marine bacteria produce polysaccharide hydrolases called ␤-agarases. ␤-Agarases A and B from Zobellia galactanivorans Dsij have recently been biochemically characterized. Here we report the first crystal structure of these two ␤-agarases. The two proteins were overproduced in Escherichia coli and crystallized, and the crystal structures were determined at 1.48 and 2.3 Å for ␤-agarases A and B, respectively. The structure of ␤-agarase A was solved by the multiple anomalous diffraction method, whereas ␤-agarase B was solved with molecular replacement using ␤-agarase A as model. Their structures adopt a jelly roll fold with a deep active site channel harboring the catalytic machinery, namely the nucleophilic residues Glu-147 and Glu-184 and the acid/ base residues Glu-152 and Glu-189 for ␤-agarases A and B, respectively. The structures of the agarases were compared with those of two lichenases and of a -carrageenase, which all belong to family 16 of the glycoside hydrolases in order to pinpoint the residues responsible for their widely differing substrate specificity. The relationship between structure and enzymatic activity of the two ␤-agarases from Z. galactanivorans Dsij was studied by analysis of the degradation products starting with different oligosaccharides. The combination of the structural and biochemical results allowed the determination of the number of subsites present in the catalytic cleft of the ␤-agarases.Agarose is a hydrophilic polysaccharide found in the cell wall of marine red algae (Rhodophyceaea) (1), where it naturally occurs in the form of a pseudocrystalline matrix associated with cellulose (2). It consists of a linear backbone of galactopyranose residues linked by alternating ␣-1,3-and ␤-1,4-linkages. Whereas the ␤-linked residues are in the D configuration, the ␣-1,3-linked galactose units are in the rare L configuration and are further modified by a 3,6-anhydro bridge (2, 3) (Fig. 1a). On the basis of x-ray fiber diffraction, optical rotation calculations, and solution gel transition, both a parallel double helix as well as a single helix structure for agarose have been proposed, where the individual polysaccharide chains have a left-handed 3-fold helix symmetry and a pitch of 1.90 nm (3, 4). Agarose forms thermo-reversible gels structured by aggregates of agarose chains. These gels exhibit unique rheological properties and are widely used as texturing agents for various applications in the food industry or as a common laboratory medium for chromatographic separation or bacterial colony growth (5).Agarases are the glycoside hydrolases (GH) 1 that hydrolyze agarose. The ␤-agarases and the ␣-agarases cleave the internal ␤-1,4-and ␣-1,3-linkage of agarose, respectively. ␤-Agarases produce agaro-oligosaccharides in the series homologous to neoagarobiose (O-3,6-anhydro-␣-L-galact...

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Section: Resultsmentioning

confidence: 73%

Section: Structural Comparison With Family Gh-16 Enzymes-mentioning

confidence: 78%

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The Three-dimensional Structures of Two β-Agarases

Allouch

Jam

Helbert

et al. 2003

Journal of Biological Chemistry

129

132

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“…Crystallographically characterized XETs and XEHs (11,45) as well as select phylogenetic Group III-A XTH gene products were also included in this analysis. The sequences of two Bacillus GH16 licheninases with known tertiary structures (47,48) were used as more distant outliers to root the phylogenetic trees. In this analysis, only the common GH16 domain was used (i.e.…”

Section: Bioinformatics Analysis Reveals a Unique Xth-like Genementioning

confidence: 99%

Structure-Function Analysis of a Broad Specificity Populus trichocarpa Endo-β-glucanase Reveals an Evolutionary Link between Bacterial Licheninases and Plant XTH Gene Products

Eklöf

Shojania

Okon

et al. 2013

Journal of Biological Chemistry

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Background: The evolution of the plant xyloglucan endotransglycosylase/hydrolase (XTH) genes in glycoside hydrolase family 16 (GH16) is enigmatic. Results: A unique, mixed function endo(xylo)glucanase from black cottonwood has been biochemically and structurally characterized. Conclusion:This enzyme is an important link between extant bacterial endoglucanases and plant XTH gene products. Significance: New insights into the molecular evolution of XTH gene products and further unification of GH16 enzymes have been gained.

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“…No cx-helical structure could be assigned. These data support the proposed all-~-structure single domain architecture for spermadhesins although does not rule out other all-13 conformations, like the jelly roll topology which appears to be a common structural motif of a variety of carbohydrate-binding proteins including legume lectins ( [17] and references therein), mammalian galectins [18,19], bacterial glucanases [20,21], human serum amyloid P component [22], and peptide : N-glycosidase F (PNGase F) from Flavobacterium menin. gosepticum [23].…”

Section: Results and ~|Onmentioning

confidence: 81%