Academic Dissertation Helsinki 2004 INTRODUCING WILSON DISEASE MUTATIONS INTO ZNTA Studies on the nucleotide and metal-binding sites of a bacterial zinc-translocating P-type ATPase
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چکیده
(2002) Introducing Wilson disease mutations into the zinc-transporting P-type ATPase of Escherichia coli. The mutation P634L in the " hinge " motif (GDGXNDXP) perturbs the formation of the E 2-P state. Eur. The nucleotide-binding domain of the Zn 2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP. Biochem. J. 377: 95-105 In addition, some unpublished data is included *) Equal contribution 5 Abbreviations A domain actuator domain ATPase adenosine triphosphatase cAPK cAMP-dependent protein kinase Cox cytochrome c oxidase GSH glutathione HAD haloacid dehalogenase IPTG isopropyl-β-D-thiogalactoside M domain membrane domain MBD metal-binding domain MNK Menkes disease protein N domain nucleotide-binding domain P domain phosphorylation domain P i inorganic phosphate PMSF phenylmethyl sulfonyl fluoride SDS sodium dodechyl sulphate SDS-PAGE sodium dodechyl sulphate polyacryl amide gel electrophoresis SOD superoxide dismutase TGN trans-Golgi network TM-helix transmembrane helix TNP-AMP trinitrophenyl adenosine monophosphate WND Wilson disease protein Wt wild-type 6
منابع مشابه
The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP.
In P-type ATPases, the nucleotide-binding (N) domain is located in the middle of the sequence which folds into the phosphorylation (P) domain. The N domain of ZntA, a Zn2+-translocating P-type ATPase from Escherichia coli, is approx. 13% identical with the N domain of sarcoplasmic reticulum Ca2+-ATPase. None of the Ca2+-ATPase residues involved in binding of ATP are found in ZntA. However, the ...
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