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- Title
Nucleotide-Binding Sites in V-Type Na+-ATPase from Enterococcus hirae1.
- Authors
Murata, Takeshi; Yoshikawa, Yasushi; Hosaka, Toshiaki; Takase, Kazuma; Kakinuma, Yoshimi; Yamato, Ichiro; Kikuchi, Takeshi
- Abstract
Enterococcus hirae V-ATPase, in contrast to most V-type ATPases, is resistant to N-ethylmaleimide (NEM). Alignment of the amino acid sequences of NtpA suggests that the NEM-sensitive Cys of V-type ATPases is replaced by Ala in E. hirae V-ATPase. Consistent with this prediction, the V-ATPase became sensitive upon substitution of the Ala with Cys. The three-dimensional structure of the NtpB subunit of V-ATPase was modeled based on the structure of the corresponding subunit (α subunit) of bovine F1-ATPase by homology modeling. Overall, the 3D structure of the subunit resembled that of a subunit of bovine F1-ATPase. The NtpB subunit, which lacks the P-loop consensus sequence for nucleotide binding, was predicted to bind a nucleotide at the modeled nucleotide-binding site. Experimental data supported the prediction that the E. hirae V-ATPase had about six nucleotide-binding sites.
- Subjects
ENTEROCOCCUS hirae; N-ethylmaleimide; NUCLEOTIDES; AMINO acid sequence; ADENOSINE triphosphatase
- Publication
Journal of Biochemistry, 2002, Vol 132, Issue 5, p789
- ISSN
0021-924X
- Publication type
Article
- DOI
10.1093/oxfordjournals.jbchem.a003288