کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2184461 1095856 2013 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
On Allosteric Modulation of P-Type Cu+-ATPases
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی بیولوژی سلول
پیش نمایش صفحه اول مقاله
On Allosteric Modulation of P-Type Cu+-ATPases
چکیده انگلیسی

P-type ATPases perform active transport of various compounds across biological membranes and are crucial for ion homeostasis and the asymmetric composition of lipid bilayers. Although their functional cycle share principles of phosphoenzyme intermediates, P-type ATPases also show subclass-specific sequence motifs and structural elements that are linked to transport specificity and mechanistic modulation. Here we provide an overview of the Cu+-transporting ATPases (of subclass PIB) and compare them to the well-studied sarco(endo)plasmic reticulum Ca2 +-ATPase (of subclass PIIA). Cu+ ions in the cell are delivered by soluble chaperones to Cu+-ATPases, which expose a putative “docking platform” at the intracellular interface. Cu+-ATPases also contain heavy-metal binding domains providing a basis for allosteric control of pump activity. Database analysis of Cu+ ligating residues questions a two-site model of intramembranous Cu+ binding, and we suggest an alternative role for the proposed second site in copper translocation and proton exchange. The class-specific features demonstrate that topological diversity in P-type ATPases may tune a general energy coupling scheme to the translocation of compounds with remarkably different properties.

Graphical AbstractFigure optionsDownload high-quality image (228 K)Download as PowerPoint slideHighlights
► Important structural differences are described between Ca2 +-ATPases and Cu+-ATPases.
► Allosteric function of the heavy-metal binding domain is suggested.
► A proposed second site in the membrane is compared to a database of copper-coordinating residues and found to be unlikely as a copper-binding site.
► The second site might be implicated as a putative site for proton exchange.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Biology - Volume 425, Issue 13, 10 July 2013, Pages 2299–2308
نویسندگان
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