Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase
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- 作者：Chao Zhaoa ; 1 ; Hiba Syeda ; Sherif S. Hassanb ; d ; Vineet K. Singhc ; Zulfiqar Ahmada ; zahmad@atsu.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：F1Fo ATP synthase ; Escherichia coli ATP synthase ; ATPase inhibition ; Oxidative phosphorylation ; Pi binding residues
- 刊名：Archives of Biochemistry and Biophysics
- 出版年：2016
- 出版时间：15 February 2016
- 年：2016
- 卷：592
- 期：Complete
- 页码：27-37
- 全文大小：3568 K
文摘
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Role of highly conserved αI346 and αI348 VISIT-DG sequence residues in Pi binding is proposed.
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Both αI346 and αI348 residues are required for upholding the phosphate binding sub-domain.
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Both αI346 and αI348 residues are required for the transition state stabilization.
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Introduction of Arg in place of Ile can compensate for the loss of an Arg involved in Pi binding.