3OHG
Crystal structure of a protein with unknown function from DUF2233 family (BACOVA_00430) from Bacteroides ovatus at 1.80 A resolution
Summary for 3OHG
| Entry DOI | 10.2210/pdb3ohg/pdb |
| Descriptor | Uncharacterized protein from DUF2233 family, CHLORIDE ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | structural genomics, unknown function, joint center for structural genomics, jcsg, protein structure initiative, psi-biology |
| Biological source | Bacteroides ovatus |
| Total number of polymer chains | 1 |
| Total formula weight | 32821.07 |
| Authors | Joint Center for Structural Genomics (JCSG) (deposition date: 2010-08-17, release date: 2010-09-08, Last modification date: 2024-11-20) |
| Primary citation | Das, D.,Lee, W.S.,Grant, J.C.,Chiu, H.J.,Farr, C.L.,Vance, J.,Klock, H.E.,Knuth, M.W.,Miller, M.D.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Kornfeld, S.,Wilson, I.A. Structure and function of the DUF2233 domain in bacteria and in the human mannose 6-phosphate uncovering enzyme. J.Biol.Chem., 288:16789-16799, 2013 Cited by PubMed Abstract: DUF2233, a domain of unknown function (DUF), is present in many bacterial and several viral proteins and was also identified in the mammalian transmembrane glycoprotein N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase ("uncovering enzyme" (UCE)). We report the crystal structure of BACOVA_00430, a 315-residue protein from the human gut bacterium Bacteroides ovatus that is the first structural representative of the DUF2233 protein family. A notable feature of this structure is the presence of a surface cavity that is populated by residues that are highly conserved across the entire family. The crystal structure was used to model the luminal portion of human UCE (hUCE), which is involved in targeting of lysosomal enzymes. Mutational analysis of several residues in a highly conserved surface cavity of hUCE revealed that they are essential for function. The bacterial enzyme (BACOVA_00430) has ∼1% of the catalytic activity of hUCE toward the substrate GlcNAc-P-mannose, the precursor of the Man-6-P lysosomal targeting signal. GlcNAc-1-P is a poor substrate for both enzymes. We conclude that, for at least a subset of proteins in this family, DUF2233 functions as a phosphodiester glycosidase. PubMed: 23572527DOI: 10.1074/jbc.M112.434977 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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