Nucleotide-binding sites in V-type Na+-ATPase from Enterococcus hirae.

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 (alpha subunit) of bovine F(1)-ATPase by homology modeling. Overall, the 3D structure of the subunit resembled that of alpha subunit of bovine F(1)-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.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Murata T,Yoshikawa Y,Hosaka T,Takase K,Kakinuma Y,Yamato I,Kikuchi T

doi

10.1093/oxfordjournals.jbchem.a003288

keywords:

subject

Has Abstract

pub_date

2002-11-01 00:00:00

pages

789-94

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

132

pub_type

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