Substrate Binding Specifically Modulates Domain Arrangements in Adenylate Kinase
نویسندگان
چکیده
منابع مشابه
The AMP - binding Domain on Adenylate Kinase
The topological location of the nucleotide substrate binding environments on adenylate kinase has been explored with the fluorescent molecule [4-benzoyl]benzoyl-1-amidofluorescein (BzAF) and the nucleotide analog 3’-0-[4-benzoyl]benzoyl-ATP (BzATP), which a re site-directed photoaffinity probes that bind covalently at the individual nucleotide sites. The MgBzATP substituted for MgATP as a subs...
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Elemental sulfur is a specific and potent inhibitor of the muscle-type isoenzyme of adenylate kinase (EC 2.7.4.3). We find inhibition by sulfur and by diadenosine pentaphosphate to be similarly potent and specific. Some properties of inhibition of adenylate kinase isoenzymes by sulfur are given. The adenylate kinase isoenzymes from skeletal muscle, brain, and heart muscle are inhibited by sulfu...
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Correlated inter-domain motions in proteins can mediate fundamental biochemical processes such as signal transduction and allostery. Here we characterize at structural level the inter-domain coupling in a multidomain enzyme, Adenylate Kinase (AK), using computational methods that exploit the shape information encoded in residual dipolar couplings (RDCs) measured under steric alignment by nuclea...
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Large conformational changes in the LID and NMP domains of adenylate kinase (AKE) are known to be key to ligand binding and catalysis, yet the order of binding events anddomainmotion is not well understood. Combining the multiple available structures for AKEwith the energy landscape theory for protein folding, a theoretical model was developed for allostery, order of binding events, and efficie...
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The cGMP-dependent protein kinase Ialpha (PKG Ialpha) possesses two functional moieties, the regulatory and catalytic domains, which reside on a single polypeptide chain. Here we report on the influence of the catalytic domain on the binding of cGMP to the regulatory domain. A deletion mutant, delta352-670 of PKG Ialpha, lacking the catalytic domain, was constructed and expressed in E. coli. Th...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2015
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2015.08.049