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4R8O

Crystal structure of a DUF3836 family protein (BVU_1206) from Bacteroides vulgatus ATCC 8482 at 2.50 A resolution

Summary for 4R8O
Entry DOI10.2210/pdb4r8o/pdb
DescriptorUncharacterized protein (2 entities in total)
Functional Keywordspf12930 family (duf3836), single layer beta sheet protein, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-biology, unknown function
Biological sourceBacteroides vulgatus
Total number of polymer chains2
Total formula weight25244.27
Authors
Joint Center for Structural Genomics (JCSG) (deposition date: 2014-09-02, release date: 2014-09-17, Last modification date: 2024-10-09)
Primary citationXu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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