Crystallization and preliminary X-ray analysis of neoagarobiose hydrolase from Saccharophagus degradans 2-40.
Many agarolytic bacteria degrade agar polysaccharide into the disaccharide unit neoagarobiose [O-3,6-anhydro-alpha-L-galactopyranosyl-(1-->3)-D-galactose] using various beta-agarases. Neoagarobiose hydrolase is an enzyme that acts on the alpha-1,3 linkage in neoagarobiose to yield D-galactose and 3,6-anhydro-L-galactose. This activity is essential in both the metabolism of agar by agarolytic bacteria and the production of fermentable sugars from agar biomass for bioenergy production. Neoagarobiose hydrolase from the marine bacterium Saccharophagus degradans 2-40 was overexpressed in Escherichia coli and crystallized in the monoclinic space group C2, with unit-cell parameters a = 129.83, b = 76.81, c = 90.11 A, beta = 101.86 degrees . The crystals diffracted to 1.98 A resolution and possibly contains two molecules in the asymmetric unit.
Lee
Saeyoung
S
School of Life Sciences and Biotechnology, Korea University, Seoul 136-713, Republic of Korea.
Lee
Jonas Yun
JY
Ha
Sung Chul
SC
Jung
Jina
J
Shin
Dong Hae
DH
Kim
Kyoung Heon
KH
Choi
In Geol
IG
D000362:Agar / Q000378:metabolism; D034241:Alteromonadaceae / Q000201:enzymology* / Q000235:genetics; D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers / Q000235:genetics; D004186:Disaccharidases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
D017931:DNA Primers; D011994:Recombinant Proteins; D000362:Agar; D004186:Disaccharidases; C039308:neoagarobiose hydrolase