Cryoelectron microscopy reveals new features in the three-dimensional structure of phosphorylase kinase

Protein Science

Volumn 14, Issue 4, 2005, Pages 914-920

  Nadeau, Owen W ^a   Gogol, Edward P ^b   Carlson, Gerald M ^a  

^a UNIVERSITY OF KANSAS SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF MISSOURI KANSAS CITY   (United States)

Author keywords

Cryoelectron microscopy; Phosphorylase kinase; Single particle analysis; Structural analysis; Three dimensional reconstruction

Indexed keywords

PHOSPHORYLASE KINASE;

ANIMAL TISSUE; ARTICLE; CRYOELECTRON MICROSCOPY; ENZYME STRUCTURE; GLYCOGENOLYSIS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MODEL; NONHUMAN; PRIORITY JOURNAL; RABBIT;

ANIMALS; CRYOELECTRON MICROSCOPY; IMAGE PROCESSING, COMPUTER-ASSISTED; MODELS, MOLECULAR; PHOSPHORYLASE KINASE; RABBITS;

EID: 15244350753     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041123905     Document Type: Article

References (18)

1. Brushia, R.J. and Walsh, D.A. 1999. Phosphorylase kinase: The complexity of its regulation is reflected in the complexity of its structure. Front. Biosci. 4: D618-D641.
2. Cohen, P. 1974. The role of phosphorylase kinase in the nervous and hormonal control of glycogenolysis in muscle. Biochem. Soc. Symp. 39: 51-73.
3. Edstrom, R.D., Meinke, M.H., Yang, X., Yang, R., and Evans, D.F. 1989. Direct observation of phosphorylase kinase and phosphorylase b by scanning tunneling microscopy. Biochemistry 28: 4939-4942.
4. Edstrom, R.D., Meinke, M.H., Yang, X., Yang, R., Elings, V., and Evans, D.F. 1990. Direct visualization of phosphorylase-phosphorylase kinase complexes by scanning tunneling and atomic force microscopy. Biophys. J. 58: 1437-1448.
5. Falke, S., Fisher, M.T., and Gogol, E.P. 2001. Structural changes in GroEL effected by binding a denatured protein substrate. J. Mol. Biol. 4: 569-577.
6. Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M., and Leith, A. 1996. SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116: 190-199.
7. 2+ as the primary cause for hysteresis in the phosphorylase kinase reactions. J. Biol. Chem. 256: 11058-11064.
8. Malhotra, A., Penczek, P., Agrawal, R.K., Gabashvili, I.S., Grassucci, R.A., Jünemann, R., Burkhardt, N., Nierhaus, K.H., and Frank, J. 1998. Escherichia coli 70S ribosome at 15 Å resolution by cryo-electron microscopy: Localization of fMet-tRNAfMet and fitting of L1 protein. J. Mol. Biol. 280: 103-116.
9. 2+-dependent global conformational change in the 3D structure of phosphorylase kinase obtained from electron microscopy. Structure 10: 23-32.
10. Norcum, M.T., Wilkinson, D.A., Carlson, M.C., Hainfeld, J.F., and Carlson, G.M. 1994. Structure of phosphorylase kinase: A three-dimensional model derived from stained and unstained electron micrographs. J. Mol. Biol. 241: 94-102.
11. 2+-induced structural changes in phosphorylase kinase detected by small angle X-ray scattering. Protein Sci. (this issue).
12. Radermacher, M., Rao, V., Grassucci, R., Frank, J., Timerman, A.P., Fleischer, S., and Wagenknecht, T. 1994. Cryo-electron microscopy and three-dimensional reconstruction of the calcium release channel/ryanodine receptor from skeletal muscle. J. Cell Biol. 127: 411-423.
13. Schramm, H.J. and Jennissen, H.P. 1985. Two-dimensional electron microscopic analysis of the chalice form of phosphorylase kinase. J. Mol. Biol. 181: 503-516.
14. Traxler, K.W., Norcum, M.T., Hainfeld, J.F., and Carlson, G.M. 2001. Direct visualization of the calmodulin subunit of phosphorylase kinase via electron microscopy following subunit exchange. J. Struct. Biol. 135: 231-238.
15. Trempe, M.R., Carlson, G.M., Hainfeld, J.F., Furcinitti, P.S., and Wall, J.S. 1986. Analyses of phosphorylase kinase by transmission and scanning transmission electron microscopy. J. Biol. Chem. 261: 2882-2889.
16. Vénien-Bryan, C., Lowe, E.M., Boisset, N., Traxler, K.W., Johnson, L.N., and Carlson, G.M. 2002. Three-dimensional structure of phosphorylase kinase at 22 Å resolution and its complex with glycogen phosphorylase b. Structure 10: 33-41.
17. Wilkinson, D.A., Marion, T.N., Tillman, D.M., Norcum, M.T., Hainfeld, J.F., Seyer, J.M., and Carlson, G.M. 1994. An epitope proximal to the carboxyl terminus of the α-subunit is located near the lobe tips of the phosphorylase kinase hexadecamer. J. Mol. Biol. 235: 974-982.
18. Wilkinson, D.A., Norcum, M.T., Fitzgerald, T.J., Marion, T.N., Tillman, D.M., and Carlson, G.M. 1997. Proximal regions of the catalytic γ and regulatory β subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation. J. Mol. Biol. 265: 319-329.