1fe6
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(New page: 200px<br /><applet load="1fe6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fe6, resolution 1.80Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 21:35, 24 November 2007
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CRYSTAL STRUCTURE OF A NATURALLY OCCURING PARALLEL RIGHT-HANDED COILED-COIL TETRAMER
Overview
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.
About this Structure
1FE6 is a Single protein structure of sequence from Staphylothermus marinus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sat Nov 24 23:42:42 2007
