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4r8o
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a DUF3836 family protein (BVU_1206) from Bacteroides vulgatus ATCC 8482 at 2.50 A resolution== | |
| + | <StructureSection load='4r8o' size='340' side='right'caption='[[4r8o]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4r8o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phocaeicola_vulgatus_ATCC_8482 Phocaeicola vulgatus ATCC 8482]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8O FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4r8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8o OCA], [https://pdbe.org/4r8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8o RCSB], [https://www.ebi.ac.uk/pdbsum/4r8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8o ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A6KZN2_PHOV8 A6KZN2_PHOV8] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Free-standing single-layer beta-sheets are extremely rare in naturally occurring proteins, even though beta-sheet motifs are ubiquitous. Here we report the crystal structures of three homologous, single-layer, anti-parallel beta-sheet proteins, comprised of three or four twisted beta-hairpin repeats. The structures reveal that, in addition to the hydrogen bond network characteristic of beta-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 beta-sheet. These new modular single-layer beta-sheet proteins may serve as a new model system for studying folding and design of beta-rich proteins. | ||
| - | + | Structures of single-layer beta-sheet proteins evolved from beta-hairpin repeats.,Xu Q, Biancalana M, Grant JC, Chiu HJ, Jaroszewski L, Knuth MW, Lesley SA, Godzik A, Elsliger MA, Deacon AM, Wilson IA Protein Sci. 2019 Sep;28(9):1676-1689. doi: 10.1002/pro.3683. Epub 2019 Aug 2. PMID:31306512<ref>PMID:31306512</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4r8o" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Phocaeicola vulgatus ATCC 8482]] | ||
Current revision
Crystal structure of a DUF3836 family protein (BVU_1206) from Bacteroides vulgatus ATCC 8482 at 2.50 A resolution
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