1vkl
From Proteopedia
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[[Category: phosphotransferase]] | [[Category: phosphotransferase]] | ||
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Revision as of 14:14, 30 October 2007
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RABBIT MUSCLE PHOSPHOGLUCOMUTASE
Overview
An electron density map of the reactive, Cd2+ form of crystalline, phosphoglucomutase from X-ray diffraction studies shows that the enzymic, phosphate donates a nonbridging oxygen to the ligand sphere of the bound, metal ion, which appears to be tetracoordinate. 31P and 113Cd NMR, spectroscopy are used to assess changes in the properties of bound Cd2+, produced by substrate/product and by substrate/product analog inhibitors., The approximately 50 ppm downfield shift of the 113Cd resonance on, formation of the complex of dephosphoenzyme and glucose 1,6-bisphosphate, is associated with the initial sugar-phosphate binding step and likely, involves a change in the geometry of the coordinating ligands. This, interpretation is supported by spectral studies involving various, complexes of the ... [(full description)]
About this Structure
1VKL is a [Single protein] structure of sequence from [Oryctolagus cuniculus] with NI as [ligand]. Active as [Phosphoglucomutase], with EC number [5.4.2.2]. Structure known Active Sites: MBA and MBB. Full crystallographic information is available from [OCA].
Reference
Structural changes at the metal ion binding site during the phosphoglucomutase reaction., Ray WJ Jr, Post CB, Liu Y, Rhyu GI, Biochemistry. 1993 Jan 12;32(1):48-57. PMID:8418859
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