Structures of two repeats of spectrin suggest models of flexibility

Valerie L. Grum; Dongning Li; Ruby I. MacDonald; Alfonso Mondragón

doi:10.1016/S0092-8674(00)81980-7

Structures of two repeats of spectrin suggest models of flexibility

Valerie L. Grum, Dongning Li, Ruby I. MacDonald, Alfonso Mondragón^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

222 Scopus citations

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 Å, 2.0 Å, 3.1 Å, and 4.0 Å resolution of two connected repeats of chicken brain α-spectrin. In all of the structures, the linker region between adjacent units is α-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.

Original language	English (US)
Pages (from-to)	523-535
Number of pages	13
Journal	Cell
Volume	98
Issue number	4
DOIs	https://doi.org/10.1016/S0092-8674(00)81980-7
State	Published - Aug 20 1999

Funding

Portions of this work were performed at the DuPont-Northwestern-Dow Collaborative Access Team (DND-CAT) Synchrotron Research Center at the APS and at SSRL. DND-CAT is supported by DuPont, Dow, the State of Illinois, and the NSF. Use of the APS is supported by the Department of Energy (DOE). SSRL is operated by the DOE, Office of Basic Energy Sciences. The SSRL Biotechnology Program is supported by the NIH and the DOE. We thank members of the Jardetzky, Mondragón, and Rosenzweig laboratories for help with data collection and A. Sharma for help in the early stages of the work; the staffs at the National Synchrotron Light Source (NSLS), the Stanford Synchrotron Radiation Labratory (SSRL), the Photon Factory (PF), and the Advanced Photon Source (APS) for their help; and S. Almo, A. Changela, H. Feinberg, S. Garman, G. Geiger, L. Godley, T. Jardetzky, R. C. MacDonald, K. Perry, A. Rosenzweig, M. Saraste, W. Weis, J. Widom, and X. Yang for their comments. We thank M. Saraste for the cDNA of chicken brain α-spectrin; M. Blum and MAR-USA for use of the CCD detector at NSLS; the Keck Foundation for resources of the Keck Facility at Northwestern University; and W. Niu for excellent technical assistance. We also thank K. Moore and L. DeLucas for help with the microgravity experiments and NASA for access to the Space Shuttle. Research was supported by a grant from the American Heart Association, Chicago Affiliate (R. I. M.), and grants from NIH (GM57692 to R. I. M. and GM51350 to A. M.).

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/S0092-8674(00)81980-7

Cite this

@article{6c3c97f8ec844909a73386fd18267843,

title = "Structures of two repeats of spectrin suggest models of flexibility",

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 {\AA}, 2.0 {\AA}, 3.1 {\AA}, and 4.0 {\AA} resolution of two connected repeats of chicken brain α-spectrin. In all of the structures, the linker region between adjacent units is α-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.",

author = "Grum, {Valerie L.} and Dongning Li and MacDonald, {Ruby I.} and Alfonso Mondrag{\'o}n",

note = "Funding Information: Portions of this work were performed at the DuPont-Northwestern-Dow Collaborative Access Team (DND-CAT) Synchrotron Research Center at the APS and at SSRL. DND-CAT is supported by DuPont, Dow, the State of Illinois, and the NSF. Use of the APS is supported by the Department of Energy (DOE). SSRL is operated by the DOE, Office of Basic Energy Sciences. The SSRL Biotechnology Program is supported by the NIH and the DOE. Funding Information: We thank members of the Jardetzky, Mondrag{\'o}n, and Rosenzweig laboratories for help with data collection and A. Sharma for help in the early stages of the work; the staffs at the National Synchrotron Light Source (NSLS), the Stanford Synchrotron Radiation Labratory (SSRL), the Photon Factory (PF), and the Advanced Photon Source (APS) for their help; and S. Almo, A. Changela, H. Feinberg, S. Garman, G. Geiger, L. Godley, T. Jardetzky, R. C. MacDonald, K. Perry, A. Rosenzweig, M. Saraste, W. Weis, J. Widom, and X. Yang for their comments. We thank M. Saraste for the cDNA of chicken brain α-spectrin; M. Blum and MAR-USA for use of the CCD detector at NSLS; the Keck Foundation for resources of the Keck Facility at Northwestern University; and W. Niu for excellent technical assistance. We also thank K. Moore and L. DeLucas for help with the microgravity experiments and NASA for access to the Space Shuttle. Research was supported by a grant from the American Heart Association, Chicago Affiliate (R. I. M.), and grants from NIH (GM57692 to R. I. M. and GM51350 to A. M.). ",

year = "1999",

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doi = "10.1016/S0092-8674(00)81980-7",

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T1 - Structures of two repeats of spectrin suggest models of flexibility

AU - Grum, Valerie L.

AU - Li, Dongning

AU - MacDonald, Ruby I.

AU - Mondragón, Alfonso

N1 - Funding Information: Portions of this work were performed at the DuPont-Northwestern-Dow Collaborative Access Team (DND-CAT) Synchrotron Research Center at the APS and at SSRL. DND-CAT is supported by DuPont, Dow, the State of Illinois, and the NSF. Use of the APS is supported by the Department of Energy (DOE). SSRL is operated by the DOE, Office of Basic Energy Sciences. The SSRL Biotechnology Program is supported by the NIH and the DOE. Funding Information: We thank members of the Jardetzky, Mondragón, and Rosenzweig laboratories for help with data collection and A. Sharma for help in the early stages of the work; the staffs at the National Synchrotron Light Source (NSLS), the Stanford Synchrotron Radiation Labratory (SSRL), the Photon Factory (PF), and the Advanced Photon Source (APS) for their help; and S. Almo, A. Changela, H. Feinberg, S. Garman, G. Geiger, L. Godley, T. Jardetzky, R. C. MacDonald, K. Perry, A. Rosenzweig, M. Saraste, W. Weis, J. Widom, and X. Yang for their comments. We thank M. Saraste for the cDNA of chicken brain α-spectrin; M. Blum and MAR-USA for use of the CCD detector at NSLS; the Keck Foundation for resources of the Keck Facility at Northwestern University; and W. Niu for excellent technical assistance. We also thank K. Moore and L. DeLucas for help with the microgravity experiments and NASA for access to the Space Shuttle. Research was supported by a grant from the American Heart Association, Chicago Affiliate (R. I. M.), and grants from NIH (GM57692 to R. I. M. and GM51350 to A. M.).

PY - 1999/8/20

Y1 - 1999/8/20

N2 - 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 Å, 2.0 Å, 3.1 Å, and 4.0 Å resolution of two connected repeats of chicken brain α-spectrin. In all of the structures, the linker region between adjacent units is α-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.

AB - 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 Å, 2.0 Å, 3.1 Å, and 4.0 Å resolution of two connected repeats of chicken brain α-spectrin. In all of the structures, the linker region between adjacent units is α-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.

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DO - 10.1016/S0092-8674(00)81980-7

M3 - Article

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AN - SCOPUS:0033588274

SN - 0092-8674

VL - 98

SP - 523

EP - 535

JO - Cell

JF - Cell

IS - 4

ER -

Structures of two repeats of spectrin suggest models of flexibility

Abstract

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CRYSTAL STRUCTURE OF REPEATS 16 AND 17 OF CHICKEN BRAIN ALPHA SPECTRIN

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Structures of two repeats of spectrin suggest models of flexibility

Abstract

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CRYSTAL STRUCTURE OF REPEATS 16 AND 17 OF CHICKEN BRAIN ALPHA SPECTRIN

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