Mitochondrial creatine kinase - A square protein

Current Opinion in Structural Biology

Volumn 7, Issue 6, 1997, Pages 811-818

  Kabsch, Wolfgang ^a   Fritz Wolf, Karin ^a  

^a MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CREATINE KINASE; GLUTAMATE AMMONIA LIGASE; GUANIDINE DERIVATIVE; MITOCHONDRIAL ENZYME;

CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STRUCTURE; MEMBRANE BINDING; PRIORITY JOURNAL; PROTEIN FAMILY; REVIEW;

EID: 0031469493     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(97)80151-0     Document Type: Article

References (39)

1. Watts DC. Creatine kinase. Boyer PD. 3 The Enzymes. 8A:1973;383-455 Academic Press, New York/London.
2. Kenyon GL, Reed GH. Creatine kinase: structure/activity relationships. Meister A. Advances in Enzymology. 54:1983;367-426 John Wiley & Sons, New York.
3. Wallimann T, Wyss M, Brdiczka D, Nicolay K, Eppenberger HM. Interacellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis. Biochem J. 281:1992;21-40.
4. Hansen DE, Knowles JR. The stereochemical course of the reaction catalysed by creatine kinase. J Biol Chem. 256:1981;5967-5969.
5. Leyh TS, Goodhart PJ, Nguyen AC, Kenyon GL, Reed GH. Structures of manganese(II) complexes with ATP, ADP, and phosphocreatine in the reactive central complexes with creatine kinase: electron paramagnetic resonance studies with oxygen-17-labeled ligands. Biochemistry. 24:1985;308-316.
6. McLaughlin AC, Leigh JS, Cohn M. Magnetic resonance study of the three-dimensional structure of creatine kinase-substrate complexes. J Biol Chem. 251:1976;2777-2787.
7. Forstner M, Kriechbaum M, Laggner P, Wallimann T. Changes of creatine kinase structure upon ligand binding as seen by small-angle scattering. of outstanding interest J Mol Struct. 383:1996;217-222 This paper reports a large reduction of the radius of gyration of mitochondrial creatine kinase upon binding of MgATP or forming a transition state analog complex.
8. Milner-White EJ, Watts DC. Inhibition of adenosine 5′-triphosphate-creatine phosphotransferase by substrate-anion complexes. Evidence for the transition-state organisation of the catalytic site. Biochem J. 122:1971;727-740.
9. Stachowiak O, Dolder M, Wallimann T. Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer. of outstanding interest Biochemistry. 35:1996;15522-15528 Using model membrane vesicles containing different amounts of cardiolipin, the authors show that only octameric mitochondrial creatine kinase induces bridged vesicle-protein complexes.
10. Beutner G, Rück A, Riede B, Welte W, Brdiczka D. Complexes between kinases, mitochondrial porin and adenylate translocator in rat brain resemble the permeability transition pore. of outstanding interest FEBS Lett. 396:1996;189-195 This paper shows that hexokinase isozyme I, as well as mitochondrial creatine kinase, exists physiologically as a complex with porin and the adenine nucleotide translocator.
11. Brdiczka D, Kaldis P, Wallimann T. In vitro complex formation between the octamer of mitochondrial creatine kinase and porin. J Biol Chem. 269:1994;27640-27644.
12. Bessman SP, Geiger PJ. Transport of energy in muscle: the phosphorylcreatine shuttle. Science. 211:1981;449-452.
13. Saks VA, Khuchua ZA, Vasilyeva EV, Belikova OY, Kuznetsov AV. Metabolic compartmentation and substrate channeling in muscle cells. Role of coupled creatine kinases in in vivo regulation of cellular respiration - a synthesis. Mol Cell Biochem. 133/134:1994;155-192.
14. Hossle JP, Schlegel J, Wegmann G, Wyss M, Böhlen P, Eppenberger HM, Wallimann T, Perriard JC. Distinct tissue specific mitochondrial creatine kinases from chicken brain and striated muscle with a conserved CK framework. Biochem Biophys Res Commun. 151:1988;408-416.
15. Mühlebach SM, Gross M, Wirz T, Wallimann T, Perriard JC, Wyss M. Sequence homology and structure predictions of the creatine kinase isozymes. Mol Cell Biochem. 133/134:1994;245-263.
16. Fritz-Wolf K, Schnyder T, Wallimann T, Kabsch W. Structure of mitochondrial creatine kinase. of outstanding interest Nature. 381:1996;341-345 This paper describes the first structure of a guanidino kinase.
17. Forstner M, Müller A, Stolz M, Wallimann T. The active site histidines of creatine kinase. A critical role of His61 situated on a flexible loop. of special interest Protein Sci. 6:1997;331-339 His61 of creatine kinase is shown to be important for the catalytic reaction but that it does not serve as an acid/base catalyst in the transphosphorylation of creatine and ATP.
18. Chen LH, Borders CL, Vásquez JR, Kenyon GL. Rabbit muscle creatine kinase: consequences of the mutagenesis of conserved histidine residues. of special interest Biochemistry. 35:1996;7895-7902 The histidine residues of rabbit muscle creatine kinase, corresponding to residues 92, 101, 186, 229, 291 in chicken mitochondrial creatine kinase, are shown not to be of importance in the transphosphorylation reaction catalysed by creatine kinase.
19. Stroud RM. Balancing ATP in the cell. of special interest Nat Struct Biol. 3:1996;567-569 Interesting views of the role and enzymatic mechanism of creatine kinase are presented.
20. Kenyon GL. Creatine kinase shapes up. of special interest Nature. 381:1996;281-282 Interesting views and comments are presented concerning the mitochondrial creatine kinase structure and the role of Cys 278 and histidines in the enzymatic mechanism.
21. Liaw SH, Jun G, Eisenberg D. Interactions of nucleotides with fully unadenylylated glutamine synthetase from Salmonella typhimurium. Biochemistry. 33:1994;11184-11188.
22. Gross M, Wallimann T. Dimer-dimer interactions in octameric mitochondrial creatine kinase. Biochemistry. 34:1995;6660-6667.
23. Gross M, Furter-Graves EM, Wallimann T, Eppenberger HM, Furter R. The tryptophan residues of mitochondrial creatine kinase: roles of Trp223, Trp206, and Trp264 in active-site and quaternary structure formation. Protein Science. 3:1994;1058-1068.
24. Kaldis P, Furter R, Wallimann T. The N-terminal heptapeptide of mitochondrial creatine kinase is important for octamerization. Biochemistry. 33:1994;952-959.
25. Schnyder T, Gross H, Winkler H, Eppenberger HM, Wallimann T. Structure of the mitochondrial creatine kinase octamer: high resolution shadowing and image averaging of single molecules and formation of linear filaments under specific staining conditions. J Cell Biol. 112:1991;95-101.
26. Schnyder T, Cyrklaff M, Fuchs K, Wallimann T. Crystallization of mitochondrial creatine kinase on negatively charged lipid bilayers. J Struct Biol. 112:1994;136-147.
27. Schnyder T, Engel A, Lustig A, Wallimann T. Native mitochondrial creatine kinase (Mi-CK) forms octameric structures. II. Characterization of dimers and octamers by ultracentrifugation, direct mass measurement by STEM and image analysis of single Mi-CK octamers. J Biol Chem. 263:1988;16954-16962.
28. Wyss M, James P, Schlegel J, Wallimann T. LImited proteolysis of creatine kinase. Implications for three-dimensional structure and for conformational substates. Biochemistry. 32:1993;10727-10735.
29. Buechter DD, Medzihradszky KF, Burlingame AL, Kenyon GL. The active site of creatine kinase. Affinity labeling of cysteine 282 with epoxycreatine. J Biol Chem. 267:1992;2173-2178.
30. Furter R, Furter-Graves EM, Wallimann T. the reactive cysteine is required for synergism but is nonessential for catalysis. Biochemistry. 32:1993;7022-7029.
31. Olcott MC, Bradley ML, Haley BE. Photoaffinity labeling of creatine kinase with 2-azido- and 8-azidoadenosine triphosphate: identifications of two peptides from the ATP-binding domain. Biochemistry. 33:1994;11935-11941.
32. James P, Wyss M, Lutsenko S, Wallimann T, Carafoli E. ATP binding site of mitochondrial creatine kinase. Affinity labelling of Asp 335 with CIRATP. FEBS Lett. 273:1990;139-143.
33. Rosevear PR, Desmeules P, Kenyon GL, Mildvan AS. Nuclear magnetic resonance studies of the role of histidines at the active site of rabbit muscle creatine kinase. Biochemistry. 20:1981;6155-6164.
34. Cook PF, Kenyon GL, Cleland WW. Use of pH studies to elucidate the catalytic mechanism of rabbit muscle creatine kinase. Biochemistry. 20:1981;1204-1210.
35. Rojo M, Hovius R, Demel RA, Nicolay K, Wallimann T. Mitochondrial creatine kinase mediates contact formation between mitochondrial membranes. J Biol Chem. 266:1991;20290-20295.
36. On enzymatic hydrolysis of PCR: a contribution to chemistry of muscle contraction Schlattner U, Forstner M, Eder M, Stachowiak O, Fritz-Wolf K, Wallimann T. Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach. of special interest Mol Cell Biochem. 1997; A detailed discussion of a possible functional role of the central channel and membrane-binding properties of mitochondrial creatine kinase.
37. Lohmann K. Über die enzymatische Aufspaltung der Creatinphosphorsäure; sugleich ein Beitrag zum Chemismus der Muskelkontraktion. Biochem Z. 271:1934;264-277.
38. Zhou G, Parthasarathy G, Somasundaram T, Abeles A, Roy L, Strong SJ, Ellington WR, Chapman MS. Expression, purification from inclusion bodies, and crystal characterization of a transition state analog complex of arginine kinase: a model for studying phosphagen kinases. of special interest Protein Sci. 6:1997;444-449 High-quality crystals of a transition state analog complex of horseshoe crab arginine kinase are described, which promise to yield important new insight into the enzyme mechanism.
39. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. 47:1991;110-119.