1fe6
From Proteopedia
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|GENE= | |GENE= | ||
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fe6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fe6 OCA], [http://www.ebi.ac.uk/pdbsum/1fe6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fe6 RCSB]</span> | ||
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[[Category: right handed coiled coil]] | [[Category: right handed coiled coil]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:21:15 2008'' |
Revision as of 17:21, 30 March 2008
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| , resolution 1.80Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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