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 Biochemjournal_title
Journal of biochemistryauthors
Murata T,Yoshikawa Y,Hosaka T,Takase K,Kakinuma Y,Yamato I,Kikuchi Tdoi
10.1093/oxfordjournals.jbchem.a003288keywords:
subject
Has Abstractpub_date
2002-11-01 00:00:00pages
789-94issue
5eissn
0021-924Xissn
1756-2651journal_volume
132pub_type
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