4COT

The importance of the Abn2 calcium cluster in the endo-1,5- arabinanase activity from Bacillus subtilis

Summary for 4COT

• Entry DOI: 10.2210/pdb4cot/pdb
• Descriptor: EXTRACELLULAR ENDO-ALPHA-(1->5)-L-ARABINANASE 2, NICKEL (II) ION, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• Functional Keywords: hydrolase, endo-alpha-l-arabinananase gh43, mutagenesis, catalytic mechanism
• Biological source: BACILLUS SUBTILIS
• Total number of polymer chains: 1
• Total formula weight: 52839.77

Authors

McVey, C.E.,Ferreira, M.J.,Correia, B.,Lahiri, S.,deSanctis, D.,Carrondo, M.A.,Lindley, P.F.,de Sa-Nogueira, I.,Soares, C.M.,Bento, I. (deposition date: 2014-01-31, release date: 2014-03-05, Last modification date: 2023-12-20)

Primary citation

Mcvey, C.E.,Ferreira, M.J.,Correia, B.,Lahiri, S.,De Sanctis, D.,Carrondo, M.A.,Lindley, P.F.,De Sa Nogueira, I.,Soares, C.M.,Bento, I.
The Importance of the Abn2 Calcium Cluster in the Endo-1,5-Arabinanase Activity from Bacillus Subtilis.
J.Biol.Inorg.Chem., 19:505-, 2014

PubMed Abstract: 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.

PubMed: 24549757
DOI: 10.1007/S00775-014-1105-X

Experimental method

X-RAY DIFFRACTION (1.9 Å)