1fe6

</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=1fe6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fe6 OCA], [https://pdbe.org/1fe6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fe6 RCSB], [https://www.ebi.ac.uk/pdbsum/1fe6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fe6 ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

The crystal structure of a polypeptide chain fragment from the surface layer protein tetrabrachion from Staphylothermus marinus has been determined at 1.8 A resolution. As proposed on the basis of the presence of 11-residue repeats, the polypeptide chain fragment forms a parallel right-handed coiled coil structure. Complementary hydrophobic interactions and complex networks of surface salt bridges result in an extremely thermostable tetrameric structure with remarkable properties. In marked contrast to left-handed coiled coil tetramers, the right-handed coiled coil reveals large hydrophobic cavities that are filled with water molecules. As a consequence, the packing of the hydrophobic core differs markedly from that of a right-handed parallel coiled coil tetramer that was designed on the basis of left-handed coiled coil structures.

Crystal structure of a naturally occurring parallel right-handed coiled coil tetramer.,Stetefeld J, Jenny M, Schulthess T, Landwehr R, Engel J, Kammerer RA Nat Struct Biol. 2000 Sep;7(9):772-6. PMID:10966648<ref>PMID:10966648</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1fe6" style="background-color:#fffaf0;"></div>

== References ==

<references/>