5NGW
Glycoside hydrolase-like protein
Summary for 5NGW
| Entry DOI | 10.2210/pdb5ngw/pdb |
| Descriptor | OpGH99A, BROMIDE ION (3 entities in total) |
| Functional Keywords | glycoside hydrolase, flavobacteria, marine polysaccharide, hydrolase |
| Biological source | Flavobacteriaceae bacterium S85 |
| Total number of polymer chains | 1 |
| Total formula weight | 44626.18 |
| Authors | Robb, C.S.,Hehemann, J.-H. (deposition date: 2017-03-20, release date: 2018-01-31, Last modification date: 2024-01-17) |
| Primary citation | Robb, C.S.,Mystkowska, A.A.,Hehemann, J.H. Crystal structure of a marine glycoside hydrolase family 99-related protein lacking catalytic machinery. Protein Sci., 26:2445-2450, 2017 Cited by PubMed Abstract: 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. PubMed: 28884852DOI: 10.1002/pro.3291 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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