Crystal structure of the actin binding domain of the cyclase-associated protein

Tetyana Dodatko, Alexander A. Fedorov, Marcin Grynberg, Yury Patskovsky, Denise A. Rozwarski, Lukasz Jaroszewski, Eliah Aronoff-Spencer, Elena Kondraskina, Tom Irving, Adam Godzik, Steven C. Almo

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Cyclase-associated protein (CAP or Srv2p) is a modular actin monomer binding protein that directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity. The crystal structure of the C-terminal dimerization and actin monomer binding domain (C-CAP) reveals a highly unusual dimer, composed of monomers possessing six coils of right-handed β-helix flanked by antiparallel β-strands. Domain swapping, involving the last two strands of each monomer, results in the formation of an extended dimer with an extensive interface. This structural and biochemical characterization provides new insights into the organization and potential mechanistic properties of the multiprotein assemblies that integrate dynamic actin processes into the overall physiology of the cell. An unanticipated finding is that the unique tertiary structure of the C-CAP monomer provides a structural model for a wide range of molecules, including RP2 and cofactor C, proteins involved in X-linked retinitis pigmentosa and tubulin maturation, respectively, as well as several uncharacterized proteins that exhibit very diverse domain organizations. Thus, the unusual right-handed β-helical fold present in C-CAP appears to support a wide range of biological functions.

Original languageEnglish (US)
Pages (from-to)10628-10641
Number of pages14
JournalBiochemistry
Volume43
Issue number33
DOIs
StatePublished - Aug 24 2004

Fingerprint

Actins
Monomers
Crystal structure
Microfilament Proteins
Cell Physiological Phenomena
Cell Polarity
Proteins
Retinitis Pigmentosa
Dimers
Structural Models
Dimerization
Tubulin
Physiology
Messenger RNA
Carrier Proteins
Molecules
tubulin-specific chaperone C

ASJC Scopus subject areas

  • Biochemistry

Cite this

Dodatko, T., Fedorov, A. A., Grynberg, M., Patskovsky, Y., Rozwarski, D. A., Jaroszewski, L., ... Almo, S. C. (2004). Crystal structure of the actin binding domain of the cyclase-associated protein. Biochemistry, 43(33), 10628-10641. https://doi.org/10.1021/bi049071r

Crystal structure of the actin binding domain of the cyclase-associated protein. / Dodatko, Tetyana; Fedorov, Alexander A.; Grynberg, Marcin; Patskovsky, Yury; Rozwarski, Denise A.; Jaroszewski, Lukasz; Aronoff-Spencer, Eliah; Kondraskina, Elena; Irving, Tom; Godzik, Adam; Almo, Steven C.

In: Biochemistry, Vol. 43, No. 33, 24.08.2004, p. 10628-10641.

Research output: Contribution to journalArticle

Dodatko, T, Fedorov, AA, Grynberg, M, Patskovsky, Y, Rozwarski, DA, Jaroszewski, L, Aronoff-Spencer, E, Kondraskina, E, Irving, T, Godzik, A & Almo, SC 2004, 'Crystal structure of the actin binding domain of the cyclase-associated protein', Biochemistry, vol. 43, no. 33, pp. 10628-10641. https://doi.org/10.1021/bi049071r
Dodatko T, Fedorov AA, Grynberg M, Patskovsky Y, Rozwarski DA, Jaroszewski L et al. Crystal structure of the actin binding domain of the cyclase-associated protein. Biochemistry. 2004 Aug 24;43(33):10628-10641. https://doi.org/10.1021/bi049071r
Dodatko, Tetyana ; Fedorov, Alexander A. ; Grynberg, Marcin ; Patskovsky, Yury ; Rozwarski, Denise A. ; Jaroszewski, Lukasz ; Aronoff-Spencer, Eliah ; Kondraskina, Elena ; Irving, Tom ; Godzik, Adam ; Almo, Steven C. / Crystal structure of the actin binding domain of the cyclase-associated protein. In: Biochemistry. 2004 ; Vol. 43, No. 33. pp. 10628-10641.
@article{1e67df7667e74cce84efb836a1464826,
title = "Crystal structure of the actin binding domain of the cyclase-associated protein",
abstract = "Cyclase-associated protein (CAP or Srv2p) is a modular actin monomer binding protein that directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity. The crystal structure of the C-terminal dimerization and actin monomer binding domain (C-CAP) reveals a highly unusual dimer, composed of monomers possessing six coils of right-handed β-helix flanked by antiparallel β-strands. Domain swapping, involving the last two strands of each monomer, results in the formation of an extended dimer with an extensive interface. This structural and biochemical characterization provides new insights into the organization and potential mechanistic properties of the multiprotein assemblies that integrate dynamic actin processes into the overall physiology of the cell. An unanticipated finding is that the unique tertiary structure of the C-CAP monomer provides a structural model for a wide range of molecules, including RP2 and cofactor C, proteins involved in X-linked retinitis pigmentosa and tubulin maturation, respectively, as well as several uncharacterized proteins that exhibit very diverse domain organizations. Thus, the unusual right-handed β-helical fold present in C-CAP appears to support a wide range of biological functions.",
author = "Tetyana Dodatko and Fedorov, {Alexander A.} and Marcin Grynberg and Yury Patskovsky and Rozwarski, {Denise A.} and Lukasz Jaroszewski and Eliah Aronoff-Spencer and Elena Kondraskina and Tom Irving and Adam Godzik and Almo, {Steven C.}",
year = "2004",
month = "8",
day = "24",
doi = "10.1021/bi049071r",
language = "English (US)",
volume = "43",
pages = "10628--10641",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "33",

}

TY - JOUR

T1 - Crystal structure of the actin binding domain of the cyclase-associated protein

AU - Dodatko, Tetyana

AU - Fedorov, Alexander A.

AU - Grynberg, Marcin

AU - Patskovsky, Yury

AU - Rozwarski, Denise A.

AU - Jaroszewski, Lukasz

AU - Aronoff-Spencer, Eliah

AU - Kondraskina, Elena

AU - Irving, Tom

AU - Godzik, Adam

AU - Almo, Steven C.

PY - 2004/8/24

Y1 - 2004/8/24

N2 - Cyclase-associated protein (CAP or Srv2p) is a modular actin monomer binding protein that directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity. The crystal structure of the C-terminal dimerization and actin monomer binding domain (C-CAP) reveals a highly unusual dimer, composed of monomers possessing six coils of right-handed β-helix flanked by antiparallel β-strands. Domain swapping, involving the last two strands of each monomer, results in the formation of an extended dimer with an extensive interface. This structural and biochemical characterization provides new insights into the organization and potential mechanistic properties of the multiprotein assemblies that integrate dynamic actin processes into the overall physiology of the cell. An unanticipated finding is that the unique tertiary structure of the C-CAP monomer provides a structural model for a wide range of molecules, including RP2 and cofactor C, proteins involved in X-linked retinitis pigmentosa and tubulin maturation, respectively, as well as several uncharacterized proteins that exhibit very diverse domain organizations. Thus, the unusual right-handed β-helical fold present in C-CAP appears to support a wide range of biological functions.

AB - Cyclase-associated protein (CAP or Srv2p) is a modular actin monomer binding protein that directly regulates filament dynamics and has been implicated in a number of complex developmental and morphological processes, including mRNA localization and the establishment of cell polarity. The crystal structure of the C-terminal dimerization and actin monomer binding domain (C-CAP) reveals a highly unusual dimer, composed of monomers possessing six coils of right-handed β-helix flanked by antiparallel β-strands. Domain swapping, involving the last two strands of each monomer, results in the formation of an extended dimer with an extensive interface. This structural and biochemical characterization provides new insights into the organization and potential mechanistic properties of the multiprotein assemblies that integrate dynamic actin processes into the overall physiology of the cell. An unanticipated finding is that the unique tertiary structure of the C-CAP monomer provides a structural model for a wide range of molecules, including RP2 and cofactor C, proteins involved in X-linked retinitis pigmentosa and tubulin maturation, respectively, as well as several uncharacterized proteins that exhibit very diverse domain organizations. Thus, the unusual right-handed β-helical fold present in C-CAP appears to support a wide range of biological functions.

UR - http://www.scopus.com/inward/record.url?scp=4143080261&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=4143080261&partnerID=8YFLogxK

U2 - 10.1021/bi049071r

DO - 10.1021/bi049071r

M3 - Article

C2 - 15311924

AN - SCOPUS:4143080261

VL - 43

SP - 10628

EP - 10641

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 33

ER -