View source for 2ww6


==foldon containing D-amino acids in turn positions==
<StructureSection load='2ww6' size='340' side='right'caption='[[2ww6]], [[Resolution|resolution]] 0.98&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ww6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WW6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.98&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=2ww6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ww6 OCA], [https://pdbe.org/2ww6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ww6 RCSB], [https://www.ebi.ac.uk/pdbsum/2ww6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ww6 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q76VI8_9CAUD Q76VI8_9CAUD] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-Turns are secondary structure elements not only exposed on protein surfaces, but also frequently found to be buried in protein-protein interfaces. Protein engineering so far considered mainly the backbone-constraining properties of synthetic beta-turn mimics as parts of surface-exposed loops. A beta-turn mimic, Hot horizontal lineTap, that is available in gram amounts, provides two hydroxyl groups that enhance its turn-inducing properties besides being able to form side-chain-like interactions. NMR studies on cyclic hexapeptides harboring the Hot horizontal lineTap dipeptide proved its strong beta-turn-inducing capability. Crystallographic analyses of the trimeric fibritin-foldon/Hot horizontal lineTap hybrid reveal at atomic resolution how Hot horizontal lineTap replaces a betaI'-turn by a betaII'-type structure. Furthermore, Hot horizontal lineTap adapts to the complex protein environment by participating in several direct and water-bridged interactions across the foldon trimer interface. As building blocks, beta-turn mimics capable of both backbone and side-chain mimicry may simplify the design of synthetic proteins.

Structural characterization of a beta-turn mimic within a protein-protein interface.,Eckhardt B, Grosse W, Essen LO, Geyer A Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18336-41. Epub 2010 Oct 11. PMID:20937907<ref>PMID:20937907</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ww6" style="background-color:#fffaf0;"></div>

==See Also==
*[[Fibritin|Fibritin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Eckhardt B]]
[[Category: Essen L-O]]
[[Category: Geyer A]]
[[Category: Grosse W]]