Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.0
Classification:STRUCTURAL PROTEIN
Release Date:1999-10-06
Deposition Date:1999-08-20
Revision Date:2008-04-27#2011-07-13
Molecular Weight:73150.12
Macromolecule Type:Protein
Residue Count:639
Atom Site Count:5136
DOI:10.2210/pdb1cun/pdb
Abstract:
Spectrin is a vital component of the cytoskeleton, conferring flexibility on cells and providing a scaffold for a variety of proteins. It is composed of tandem, antiparallel coiled-coil repeats. We report four related crystal structures at 1.45 A, 2.0 A, 3.1 A, and 4.0 A resolution of two connected repeats of chicken brain alpha-spectrin. In all of the structures, the linker region between adjacent units is alpha-helical without breaks, kinks, or obvious boundaries. Two features observed in the structures are (1) conformational rearrangement in one repeat, resulting in movement of the position of a loop, and (2) varying degrees of bending at the linker region. These features form the basis of two different models of flexibility: a conformational rearrangement and a bending model. These models provide novel atomic details of spectrin flexibility.
Resolution:2.0
Classification:STRUCTURAL PROTEIN
Release Date:1999-10-06
Deposition Date:1999-08-20
Revision Date:2008-04-27#2011-07-13
Molecular Weight:73150.12
Macromolecule Type:Protein
Residue Count:639
Atom Site Count:5136
DOI:10.2210/pdb1cun/pdb
Abstract:
Spectrin is a vital component of the cytoskeleton, conferring flexibility on cells and providing a scaffold for a variety of proteins. It is composed of tandem, antiparallel coiled-coil repeats. We report four related crystal structures at 1.45 A, 2.0 A, 3.1 A, and 4.0 A resolution of two connected repeats of chicken brain alpha-spectrin. In all of the structures, the linker region between adjacent units is alpha-helical without breaks, kinks, or obvious boundaries. Two features observed in the structures are (1) conformational rearrangement in one repeat, resulting in movement of the position of a loop, and (2) varying degrees of bending at the linker region. These features form the basis of two different models of flexibility: a conformational rearrangement and a bending model. These models provide novel atomic details of spectrin flexibility.
Date made available | 1999 |
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Publisher | RCSB-PDB |