Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIα, and truncated CaM kinase IIα reveal a unique organization for its structural core and functional domains

Steven J. Kolodziej, Andy Hudmon, M. Neal Waxham, James K. Stoops

Research output: Contribution to journalArticle

127 Citations (Scopus)

Abstract

Studies of the structural organization of calcium/calmodulin-dependent protein kinase IIα (CaM KIIα) and truncated CaM KIIα by three-dimensional electron microscopy and protein engineering show that the structures consist of 12 subunits that are organized in two stacked hexameric rings with 622 symmetry. The body of CaM KIIα is gear-shaped, consisting of six slanted flanges, and has six foot-like processes attached by narrow appendages to both ends of the flanges. Truncated CaM KIIα that lacks functional domains has a structure that is very similar to the body of CaM KIIα. Thus, the functional domains reside in the foot-like processes, and the association domain comprises the gear-shaped core. The ribbon diagram of the bilobate structure of CaM KI fits nicely in the envelope of the foot-like component and indicates that the crevice between the two lobes comprising the functional domains is near the middle portion of the foot. The clustering of the functional domains provides a favorable arrangement for the autophosphorylation reaction, and the unusual arrangement of the catalytic domain on extended tethers appears to be significant for the remarkable functional diversity of CaM KIIα in cellular regulation.

Original languageEnglish (US)
Pages (from-to)14354-14359
Number of pages6
JournalJournal of Biological Chemistry
Volume275
Issue number19
DOIs
StatePublished - May 12 2000
Externally publishedYes

Fingerprint

Calcium-Calmodulin-Dependent Protein Kinases
Calmodulin
Phosphotransferases
Calcium
Foot
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Flanges
Gears
Protein Engineering
Electron microscopy
Cluster Analysis
Catalytic Domain
Electron Microscopy
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIα, and truncated CaM kinase IIα reveal a unique organization for its structural core and functional domains. / Kolodziej, Steven J.; Hudmon, Andy; Waxham, M. Neal; Stoops, James K.

In: Journal of Biological Chemistry, Vol. 275, No. 19, 12.05.2000, p. 14354-14359.

Research output: Contribution to journalArticle

@article{4a375400499248f9bbcecce39f09fd27,
title = "Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIα, and truncated CaM kinase IIα reveal a unique organization for its structural core and functional domains",
abstract = "Studies of the structural organization of calcium/calmodulin-dependent protein kinase IIα (CaM KIIα) and truncated CaM KIIα by three-dimensional electron microscopy and protein engineering show that the structures consist of 12 subunits that are organized in two stacked hexameric rings with 622 symmetry. The body of CaM KIIα is gear-shaped, consisting of six slanted flanges, and has six foot-like processes attached by narrow appendages to both ends of the flanges. Truncated CaM KIIα that lacks functional domains has a structure that is very similar to the body of CaM KIIα. Thus, the functional domains reside in the foot-like processes, and the association domain comprises the gear-shaped core. The ribbon diagram of the bilobate structure of CaM KI fits nicely in the envelope of the foot-like component and indicates that the crevice between the two lobes comprising the functional domains is near the middle portion of the foot. The clustering of the functional domains provides a favorable arrangement for the autophosphorylation reaction, and the unusual arrangement of the catalytic domain on extended tethers appears to be significant for the remarkable functional diversity of CaM KIIα in cellular regulation.",
author = "Kolodziej, {Steven J.} and Andy Hudmon and Waxham, {M. Neal} and Stoops, {James K.}",
year = "2000",
month = "5",
day = "12",
doi = "10.1074/jbc.275.19.14354",
language = "English (US)",
volume = "275",
pages = "14354--14359",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "19",

}

TY - JOUR

T1 - Three-dimensional reconstructions of calcium/calmodulin-dependent (CaM) kinase IIα, and truncated CaM kinase IIα reveal a unique organization for its structural core and functional domains

AU - Kolodziej, Steven J.

AU - Hudmon, Andy

AU - Waxham, M. Neal

AU - Stoops, James K.

PY - 2000/5/12

Y1 - 2000/5/12

N2 - Studies of the structural organization of calcium/calmodulin-dependent protein kinase IIα (CaM KIIα) and truncated CaM KIIα by three-dimensional electron microscopy and protein engineering show that the structures consist of 12 subunits that are organized in two stacked hexameric rings with 622 symmetry. The body of CaM KIIα is gear-shaped, consisting of six slanted flanges, and has six foot-like processes attached by narrow appendages to both ends of the flanges. Truncated CaM KIIα that lacks functional domains has a structure that is very similar to the body of CaM KIIα. Thus, the functional domains reside in the foot-like processes, and the association domain comprises the gear-shaped core. The ribbon diagram of the bilobate structure of CaM KI fits nicely in the envelope of the foot-like component and indicates that the crevice between the two lobes comprising the functional domains is near the middle portion of the foot. The clustering of the functional domains provides a favorable arrangement for the autophosphorylation reaction, and the unusual arrangement of the catalytic domain on extended tethers appears to be significant for the remarkable functional diversity of CaM KIIα in cellular regulation.

AB - Studies of the structural organization of calcium/calmodulin-dependent protein kinase IIα (CaM KIIα) and truncated CaM KIIα by three-dimensional electron microscopy and protein engineering show that the structures consist of 12 subunits that are organized in two stacked hexameric rings with 622 symmetry. The body of CaM KIIα is gear-shaped, consisting of six slanted flanges, and has six foot-like processes attached by narrow appendages to both ends of the flanges. Truncated CaM KIIα that lacks functional domains has a structure that is very similar to the body of CaM KIIα. Thus, the functional domains reside in the foot-like processes, and the association domain comprises the gear-shaped core. The ribbon diagram of the bilobate structure of CaM KI fits nicely in the envelope of the foot-like component and indicates that the crevice between the two lobes comprising the functional domains is near the middle portion of the foot. The clustering of the functional domains provides a favorable arrangement for the autophosphorylation reaction, and the unusual arrangement of the catalytic domain on extended tethers appears to be significant for the remarkable functional diversity of CaM KIIα in cellular regulation.

UR - http://www.scopus.com/inward/record.url?scp=0034640259&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0034640259&partnerID=8YFLogxK

U2 - 10.1074/jbc.275.19.14354

DO - 10.1074/jbc.275.19.14354

M3 - Article

VL - 275

SP - 14354

EP - 14359

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 19

ER -