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Crystal structure of a marine glycoside hydrolase family 99‐related protein lacking catalytic machinery
Author(s) -
Robb Craig S.,
Mystkowska Agata Anna,
Hehemann JanHendrik
Publication year - 2017
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3291
Subject(s) - glycoside hydrolase , hydrolase , biochemistry , protein family , polysaccharide , structural genomics , biology , flavobacterium , chemistry , protein structure , enzyme , bacteria , gene , genetics , pseudomonas
Algal polysaccharides of diverse structures are one of the most abundant carbon resources for heterotrophic, marine bacteria with coevolved digestive enzymes. A putative sulfo‐mannan polysaccharide utilization locus, which is conserved in marine flavobacteria, contains an unusual GH99‐like protein that lacks the conserved catalytic residues of glycoside hydrolase family 99. Using X‐ray crystallography, we structurally characterized this protein from the marine flavobacterium Ochrovirga pacifica to help elucidate its molecular function. The structure reveals the absence of potential catalytic residues for polysaccharide hydrolysis, which—together with additional structural features—suggests this protein may be noncatalytic and involved in carbohydrate binding.