Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of A1-III from a Sphingomonas species A1 complexed with a trisaccharide product (4-deoxy-l-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid) was determined by X-ray crystallography at 2.0 A with an R-factor of 0.16. The final model of the complex form comprising 351 amino acid residues, 245 water molecules, one sulfate ion and one trisaccharide product exhibited a C(alpha) r.m.s.d. value of 0.154 A with the reported apo form of the enzyme. The trisaccharide was bound in the active cleft at subsites -3 approximately -1 from the non-reducing end by forming several hydrogen bonds and van der Waals interactions with protein atoms. The catalytic residue was estimated to be Tyr246, which existed between subsites -1 and +1 based on a mannuronic acid model oriented at subsite +1.
Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 A resolution.,Yoon HJ, Hashimoto W, Miyake O, Murata K, Mikami B J Mol Biol. 2001 Mar 16;307(1):9-16. PMID:11243798[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yoon HJ, Hashimoto W, Miyake O, Murata K, Mikami B. Crystal structure of alginate lyase A1-III complexed with trisaccharide product at 2.0 A resolution. J Mol Biol. 2001 Mar 16;307(1):9-16. PMID:11243798 doi:http://dx.doi.org/10.1006/jmbi.2000.4509
