3OHG

Crystal structure of a protein with unknown function from DUF2233 family (BACOVA_00430) from Bacteroides ovatus at 1.80 A resolution

3OHG の概要

• エントリーDOI: 10.2210/pdb3ohg/pdb
• 分子名称: Uncharacterized protein from DUF2233 family, CHLORIDE ION, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: structural genomics, unknown function, joint center for structural genomics, jcsg, protein structure initiative, psi-biology
• 由来する生物種: Bacteroides ovatus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32821.07

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2010-08-17, 公開日: 2010-09-08, 最終更新日: 2024-11-20)

主引用文献

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

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: 23572527
DOI: 10.1074/jbc.M112.434977

実験手法

X-RAY DIFFRACTION (1.8 Å)