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 1.80&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1fe6.jpg|left|200px]]<br /><applet load="1fe6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fe6, resolution 1.80&Aring;" />
caption="1fe6, resolution 1.80&Aring;" />
'''CRYSTAL STRUCTURE OF A NATURALLY OCCURING PARALLEL RIGHT-HANDED COILED-COIL TETRAMER'''<br />
'''CRYSTAL STRUCTURE OF A NATURALLY OCCURING PARALLEL RIGHT-HANDED COILED-COIL TETRAMER'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1FE6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylothermus_marinus Staphylothermus marinus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FE6 OCA].
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1FE6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylothermus_marinus Staphylothermus marinus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FE6 OCA].
==Reference==
==Reference==
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[[Category: right handed coiled coil]]
[[Category: right handed coiled coil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:42:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:46 2008''

Revision as of 10:37, 21 February 2008


1fe6, resolution 1.80Å

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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

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