5lo3
From Proteopedia
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==Engineering protein stability with atomic precision in a monomeric miniprotein== | ==Engineering protein stability with atomic precision in a monomeric miniprotein== | ||
| - | <StructureSection load='5lo3' size='340' side='right' caption='[[5lo3 | + | <StructureSection load='5lo3' size='340' side='right'caption='[[5lo3]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5lo3]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LO3 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5lo3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LO3 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0A1:O-METHYL-L-TYROSINE'>0A1</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</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=5lo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lo3 OCA], [https://pdbe.org/5lo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lo3 RCSB], [https://www.ebi.ac.uk/pdbsum/5lo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lo3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SPAP_STRMU SPAP_STRMU] Surface protein antigen implicated in dental caries. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Miniproteins simplify the protein-folding problem, allowing the dissection of forces that stabilize protein structures. Here we describe PPalpha-Tyr, a designed peptide comprising an alpha-helix buttressed by a polyproline II helix. PPalpha-Tyr is water soluble and monomeric, and it unfolds cooperatively with a midpoint unfolding temperature (TM) of 39 degrees C. NMR structures of PPalpha-Tyr reveal proline residues docked between tyrosine side chains, as designed. The stability of PPalpha is sensitive to modifications in the aromatic residues: replacing tyrosine with phenylalanine, i.e., changing three solvent-exposed hydroxyl groups to protons, reduces the TM to 20 degrees C. We attribute this result to the loss of CH-pi interactions between the aromatic and proline rings, which we probe by substituting the aromatic residues with nonproteinogenic side chains. In analyses of natural protein structures, we find a preference for proline-tyrosine interactions over other proline-containing pairs, and observe abundant CH-pi interactions in biologically important complexes between proline-rich ligands and SH3 and similar domains. | ||
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| + | Engineering protein stability with atomic precision in a monomeric miniprotein.,Baker EG, Williams C, Hudson KL, Bartlett GJ, Heal JW, Porter Goff KL, Sessions RB, Crump MP, Woolfson DN Nat Chem Biol. 2017 Jul;13(7):764-770. doi: 10.1038/nchembio.2380. Epub 2017 May , 22. PMID:28530710<ref>PMID:28530710</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5lo3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Streptococcus mutans]] |
| - | [[Category: | + | [[Category: Baker EG]] |
| - | [[Category: | + | [[Category: Bartlett GG]] |
| - | [[Category: | + | [[Category: Crump MP]] |
| - | [[Category: | + | [[Category: Heal JW]] |
| - | [[Category: | + | [[Category: Hudson KL]] |
| - | [[Category: | + | [[Category: Sessions RB]] |
| - | [[Category: | + | [[Category: Williams C]] |
| - | [[Category: | + | [[Category: Woolfson DN]] |
Current revision
Engineering protein stability with atomic precision in a monomeric miniprotein
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