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Titolo:
Crystal structure of brain-type creatine kinase at 1.41 angstrom resolution
Autore:
Eder, M; Schlattner, U; Becker, A; Wallimann, T; Kabsch, W; Fritz-Wolf, K;
Indirizzi:
Max Planck Inst Med Res, Dept Biophys, D-69120 Heidelberg, Germany Max Planck Inst Med Res Heidelberg Germany D-69120 0 Heidelberg, Germany ETH Zurich, Inst Cell Biol, CH-8093 Zurich, Switzerland ETH Zurich Zurich Switzerland CH-8093 Biol, CH-8093 Zurich, Switzerland
Titolo Testata:
PROTEIN SCIENCE
fascicolo: 11, volume: 8, anno: 1999,
pagine: 2258 - 2269
SICI:
0961-8368(199911)8:11<2258:CSOBCK>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
DIFFRACTION DATA; ACTIVE-SITE; STRUCTURE REFINEMENT; SECONDARY STRUCTURE; RAT UTERUS; PROTEIN; ISOENZYMES; IDENTIFICATION; LOCALIZATION; EXPRESSION;
Keywords:
brain-type creatine kinase; cancer; cellular energy metabolism; guanidino kinase; neurodegenerative disorders;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
76
Recensione:
Indirizzi per estratti:
Indirizzo: Kabsch, W Max Planck Inst Med Res, Dept Biophys, Jahnstr 29, D-69120 Heidelberg, Germany Max Planck Inst Med Res Jahnstr 29 Heidelberg Germany D-69120 y
Citazione:
M. Eder et al., "Crystal structure of brain-type creatine kinase at 1.41 angstrom resolution", PROTEIN SCI, 8(11), 1999, pp. 2258-2269

Abstract

Excitable cells and tissues like muscle or brain show a highly fluctuatingconsumption of ATP, which is efficiently regenerated from a large pool of phosphocreatine by the enzyme creatine kinase (CK). The enzyme exists in tissue-as well as compartment-specific isoforms. Numerous pathologies are related to the CK system: CK is found to be overexpressed in a wide range of solid tumors, whereas functional impairment of CK leads to a deterioration in energy metabolism. which is phenotypic for many neurodegenerative and age-related diseases. The crystal structure of chicken cytosolic brain-type creatine kinase (BB-CK) has been served to 1.41 Angstrom resolution by molecular replacement. It represents the most accurately determined structure in the family of guanidino kinases. Except for the N-terminal region (2-12), the structures of both monomers in the biological dimer are very similar andclosely resemble those of the other known structures in the family. Specific Ca2+-mediated interactions, found between two dimers in the asymmetric unit, result in structurally independent heterodimers differing in their N-terminal conformation and secondary structure. The high-resolution structureof BB-CK presented in this work will assist in designing new experiments to reveal the molecular basis of the multiple isoform-specific properties ofCK, especially regarding different subcellular locations and functional interactions with other proteins. The rather similar fold shared by all knownguanidino kinase structures suggests a model for the transition state complex of BB-CK analogous to the one of arginine kinase (AK). Accordingly, we have modeled a putative conformation of CK in the transition state that requires a rigid body movement of the entire N-terminal domain by rms 4 Angstrom from the structure without substrates.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 01:53:29