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3msw

From Proteopedia

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{{STRUCTURE_3msw| PDB=3msw | SCENE= }}
 
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===Crystal structure of a Protein with unknown function (BF3112) from Bacteroides fragilis NCTC 9343 at 1.90 A resolution===
 
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==About this Structure==
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==Crystal structure of a Protein with unknown function (BF3112) from Bacteroides fragilis NCTC 9343 at 1.90 A resolution==
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[[3msw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MSW OCA].
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<StructureSection load='3msw' size='340' side='right'caption='[[3msw]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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[[Category: Bacteroides fragilis]]
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== Structural highlights ==
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[[Category: JCSG, Joint Center for Structural Genomics.]]
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<table><tr><td colspan='2'>[[3msw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis_NCTC_9343 Bacteroides fragilis NCTC 9343]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MSW FirstGlance]. <br>
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[[Category: Jcsg]]
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PGR:R-1,2-PROPANEDIOL'>PGR</scene></td></tr>
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[[Category: Joint center for structural genomic]]
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3msw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3msw OCA], [https://pdbe.org/3msw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3msw RCSB], [https://www.ebi.ac.uk/pdbsum/3msw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3msw ProSAT]</span></td></tr>
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[[Category: Protein structure initiative]]
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</table>
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[[Category: Psi-2]]
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== Function ==
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[[Category: Structural genomic]]
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[https://www.uniprot.org/uniprot/Q5LAR6_BACFN Q5LAR6_BACFN]
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[[Category: Unknown function]]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ms/3msw_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3msw ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3msw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacteroides fragilis NCTC 9343]]
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[[Category: Large Structures]]

Current revision

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

PDB ID 3msw

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