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  Crystal structure of human ubiquitous mitochondrial creatine kinase

Eder, M., Fritz-Wolf, K., Kabsch, W., Wallimann, T., & Schlattner, U. (2000). Crystal structure of human ubiquitous mitochondrial creatine kinase. Proteins: Structure, Function, and Bioinformatics, 39(3), 216-225. doi:10.1002/(SICI)1097-0134(20000515)39:3<216:AID-PROT40>3.0.CO;2-#.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-AE73-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-AE74-B
Genre: Journal Article
Alternative Title : Crystal structure of human ubiquitous mitochondrial creatine kinase

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Proteins_39_2000_216.pdf (Any fulltext), 491KB
 
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 Creators:
Eder, Michael1, Author              
Fritz-Wolf, Karin1, Author              
Kabsch, Wolfgang1, Author              
Wallimann, Theo, Author
Schlattner, Uwe, Author
Affiliations:
1Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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Free keywords: guanidino kinases; oligomeric protein; cellular energy metabolism; membrane binding
 Abstract: Creatine kinase (CK), catalyzing the reversible trans-phosphorylation between ATP and creatine, plays a key role in the energy metabolism of cells with high and fluctuating energy requirements. We have solved the X-ray structure of octameric human ubiquitous mitochondrial CK (uMtCK) at 2.7 ? resolution, representing the first human CK structure. The structure is very similar to the previously determined structure of sarcomeric mitochondrial CK (sMtCK). The cuboidal octamer has 422 point group symmetry with four dimers arranged along the fourfold axis and a central channel of 20 ? diameter, which extends through the whole octamer. Structural differences with respect to sMtCK are found in isoform-specific regions important for octamer formation and membrane binding. Octameric uMtCK is stabilized by numerous additional polar interactions between the N-termini of neighboring dimers, which extend into the central channel and form clamp-like structures, and by a pair of salt bridges in the hydrophobic interaction patch. The five C-terminal residues of uMtCK, carrying positive charges likely to be involved in phospholipid-binding, are poorly defined by electron density, indicating a more flexible region than the corresponding one in sMtCK. The structural differences between uMtCK and sMtCK are consistent with biochemical studies on octamer stability and membrane binding of the two isoforms

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Language(s): eng - English
 Dates: 1999-08-201999-12-202000-03-242000-05-15
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Proteins: Structure, Function, and Bioinformatics
Source Genre: Journal
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Publ. Info: New York, NY : John Wiley & Sons
Pages: - Volume / Issue: 39 (3) Sequence Number: - Start / End Page: 216 - 225 Identifier: ISSN: 0887-3585
CoNE: https://pure.mpg.de/cone/journals/resource/954925553393_1