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  Crystal structure of brain-type creatine kinase at 1.41 Å resolution

Eder, M., Schlattner, U., Becker, A., Wallimann, T., Kabsch, W., & Fritz-Wolf, K. (1999). Crystal structure of brain-type creatine kinase at 1.41 Å resolution. Protein Science, 8(11), 2258-2269. doi:10.1110/ps.8.11.2258.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-55B7-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-55B8-2
Genre: Journal Article
Alternative Title : Crystal structure of brain-type creatine kinase at 1.41 Å resolution

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ProtSci_8_1999_2524.pdf (Any fulltext), 162KB
 
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 Creators:
Eder, Michael, Author
Schlattner, Uwe, Author
Becker, Andreas1, Author              
Wallimann, Theo, Author
Kabsch, Wolfgang1, 2, Author              
Fritz-Wolf, Karin2, Author              
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              
2Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: brain-type creatine kinase; cancer; cellular energy metabolism; guanidino kinase; neurodegenerative disorders
 Abstract: Excitable cells and tissues like muscle or brain show a highly fluctuating consumption 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 solved to 1.41 A 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 and closely 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 structure of BB-CK presented in this work will assist in designing new experiments to reveal the molecular basis of the multiple isoform-specific properties of CK, especially regarding different subcellular locations and functional interactions with other proteins. The rather similar fold shared by all known guanidino 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 A from the structure without substrates

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Language(s): eng - English
 Dates: 1999-05-171999-07-231999-11
 Publication Status: Published in print
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 666610
DOI: 10.1110/ps.8.11.2258
URI: http://www.ncbi.nlm.nih.gov/pubmed/10595529
Other: 4396
 Degree: -

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Title: Protein Science
Source Genre: Journal
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Publ. Info: New York, N.Y. : Cambridge University Press
Pages: - Volume / Issue: 8 (11) Sequence Number: - Start / End Page: 2258 - 2269 Identifier: ISSN: 0961-8368
CoNE: https://pure.mpg.de/cone/journals/resource/954925342760