5lo3: Difference between revisions
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The | ==Engineering protein stability with atomic precision in a monomeric miniprotein== | ||
<StructureSection load='5lo3' size='340' side='right'caption='[[5lo3]]' scene=''> | |||
== Structural highlights == | |||
<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr> | |||
<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> | |||
== 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. | |||
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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5lo3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus mutans]] | |||
[[Category: Baker EG]] | |||
[[Category: Bartlett GG]] | |||
[[Category: Crump MP]] | |||
[[Category: Heal JW]] | |||
[[Category: Hudson KL]] | |||
[[Category: Sessions RB]] | |||
[[Category: Williams C]] | |||
[[Category: Woolfson DN]] | |||
