4R03

Crystal structure of a DUF3836 family protein (BDI_3222) from Parabacteroides distasonis ATCC 8503 at 1.50 A resolution

4R03 の概要

• エントリーDOI: 10.2210/pdb4r03/pdb
• 分子名称: Uncharacterized protein, (4S)-2-METHYL-2,4-PENTANEDIOL, CITRIC ACID, ... (5 entities in total)
• 機能のキーワード: pf12930 family protein, duf3836, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, unknown function
• 由来する生物種: Parabacteroides distasonis ATCC 8503
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13772.66

構造登録者

Joint Center for Structural Genomics (JCSG) (登録日: 2014-07-29, 公開日: 2014-08-27, 最終更新日: 2024-11-06)

主引用文献

Xu, Q.,Biancalana, M.,Grant, J.C.,Chiu, H.J.,Jaroszewski, L.,Knuth, M.W.,Lesley, S.A.,Godzik, A.,Elsliger, M.A.,Deacon, A.M.,Wilson, I.A.
Structures of single-layer beta-sheet proteins evolved from beta-hairpin repeats.
Protein Sci., 28:1676-1689, 2019

PubMed Abstract: Free-standing single-layer β-sheets are extremely rare in naturally occurring proteins, even though β-sheet motifs are ubiquitous. Here we report the crystal structures of three homologous, single-layer, anti-parallel β-sheet proteins, comprised of three or four twisted β-hairpin repeats. The structures reveal that, in addition to the hydrogen bond network characteristic of β-sheets, additional hydrophobic interactions mediated by small clusters of residues adjacent to the turns likely play a significant role in the structural stability and compensate for the lack of a compact hydrophobic core. These structures enabled identification of a family of secreted proteins that are broadly distributed in bacteria from the human gut microbiome and are putatively involved in the metabolism of complex carbohydrates. A conserved surface patch, rich in solvent-exposed tyrosine residues, was identified on the concave surface of the β-sheet. These new modular single-layer β-sheet proteins may serve as a new model system for studying folding and design of β-rich proteins.

PubMed: 31306512
DOI: 10.1002/pro.3683

実験手法

X-RAY DIFFRACTION (1.5 Å)