3MSW

Crystal structure of a Protein with unknown function (BF3112) from Bacteroides fragilis NCTC 9343 at 1.90 A resolution

Summary for 3MSW

• Entry DOI: 10.2210/pdb3msw/pdb
• Descriptor: uncharacterized protein, CHLORIDE ION, R-1,2-PROPANEDIOL, ... (4 entities in total)
• Functional Keywords: structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, unknown function
• Biological source: Bacteroides fragilis
• Total number of polymer chains: 1
• Total formula weight: 17553.17

Authors

Joint Center for Structural Genomics (JCSG) (deposition date: 2010-04-29, release date: 2010-06-09, Last modification date: 2023-02-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)