TY - JOUR
T1 - The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis
AU - McVey, C E
AU - Correia, B
AU - Lahiri, S
AU - de Sanctis, D
AU - Carrondo, Maria Arménia
AU - Lindley, P F
AU - Sá Nogueira, Isabel Maria Godinho de
AU - Soares, Cláudio Manuel
AU - Bento, Isabel
N1 - WOS:000336310000003
PY - 2014/6
Y1 - 2014/6
N2 - Arabinanase is a glycosyl hydrolase that is able to cleave the glycosidic bonds of α-1,5-L-arabinan, releasing arabino-oligosaccharides and L-arabinose. The enzyme has two domains, an N-terminal catalytic domain with a characteristic β-propeller fold and a C-terminal domain whose function is unknown. A calcium ion, located near the catalytic site, serves to stabilize the N-terminal domain, but it has also been proposed to play a key role in the enzyme mechanism. The present work describes the structure of an inactive mutant of the wild-type enzyme (H318Q) and in which the calcium ion has been adventitiously replaced by nickel. These structural studies, together with functional and modelling studies, clearly support the role of the calcium ion in the overall reaction mechanism.
AB - Arabinanase is a glycosyl hydrolase that is able to cleave the glycosidic bonds of α-1,5-L-arabinan, releasing arabino-oligosaccharides and L-arabinose. The enzyme has two domains, an N-terminal catalytic domain with a characteristic β-propeller fold and a C-terminal domain whose function is unknown. A calcium ion, located near the catalytic site, serves to stabilize the N-terminal domain, but it has also been proposed to play a key role in the enzyme mechanism. The present work describes the structure of an inactive mutant of the wild-type enzyme (H318Q) and in which the calcium ion has been adventitiously replaced by nickel. These structural studies, together with functional and modelling studies, clearly support the role of the calcium ion in the overall reaction mechanism.
KW - Bacillus subtilis
KW - Calcium
KW - Catalysis
KW - Catalytic Domain
KW - Crystallography, X-Ray
KW - Glycoside Hydrolases
KW - Models, Molecular
KW - Mutagenesis, Site-Directed
KW - Substrate Specificity
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
U2 - 10.1007/s00775-014-1105-x
DO - 10.1007/s00775-014-1105-x
M3 - Article
C2 - 24549757
VL - 19
SP - 505
EP - 513
JO - Journal Of Biological Inorganic Chemistry
JF - Journal Of Biological Inorganic Chemistry
SN - 0949-8257
IS - 4-5
ER -