http://www.cnr.it/ontology/cnr/individuo/prodotto/ID79023
Structural and functional studies of carbohydrate esterase family 7 enzymes (Contributo in atti di convegno)
- Type
- Label
- Structural and functional studies of carbohydrate esterase family 7 enzymes (Contributo in atti di convegno) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
- Alternative label
I. Krastanova, A. Cassetta, D. Lamba (2005)
Structural and functional studies of carbohydrate esterase family 7 enzymes
in XX Congress of the International Union of Crystallography, Florence, 2005
(literal)
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- I. Krastanova, A. Cassetta, D. Lamba (literal)
- Pagina inizio
- Pagina fine
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- Rivista
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- XX Congress of the International Union of Crystallography:
Congress and General Assembly
23-31 August 2005
Acta Cryst. (2005) A61, c208
(literal)
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- I. Krastanova -SISSA, Trieste
A. Cassetta -IC-CNR, Trieste
D. Lamba -IC-CNR, Trieste (literal)
- Titolo
- Structural and functional studies of carbohydrate esterase family 7 enzymes (literal)
- Abstract
- The Carbohydrate Esterase family 7 (CE-7, CAZy, April 2005)
includes 26 bacterial oligomeric ?/? hydrolases with multifunctional
deacetylase activity. Their primary role is the deacetylation of the
decorated xylooligosaccharides that are transported into the bacterium
cytoplasm. Therefore, the enzymes could be considered accessory
ones in the plant cell wall biodegradation. Despite the crystal structure
of two family members was determined, it is still unclear how the
substrate reaches the catalytic site, and how the product is released
from the oligomeric enzymatic assembly. To further characterize the
CE-7 family, Bacillus pumilus acetyl xylan esterase (AXE) was
expressed, purified and crystallized - alone and in complex with the
reaction products xylose and acetate. The 3D structures were
determined by X-ray analysis at 1.9Å and 2.6Å respectively, each one
showing two doughnut-like hexamers with local 32 symmetry in the
asymmetric unit. Snapshots of the enzymatic process were obtained.
The identified xylose binding sites let us hypothesize a route
connecting the active site to the exterior of the selfcompartmentalizing
enzymatic assembly. The CE-7 family
representative, Thermoanaerobacterium sp. AXE1, was also
characterized, and its crystal structure determined at 1.9Å. As a result,
new insights into the CE-7 family mechanism of action are suggested,
and structural basis for their different sensitivity to the commonly
used serine-modifying reagent, PMSF, are provided. (literal)
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