1iqs
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(New page: 200px<br /><applet load="1iqs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iqs" /> '''Minimized average structure of MTH1880 from ...)
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Revision as of 20:15, 24 November 2007
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Minimized average structure of MTH1880 from Methanobacterium Thermoautotrophicum
Overview
MTH1880 is a hypothetical protein from Methanobacterium, thermoautotrophicum, a target organism of structural genomics. The, solution structure determined by NMR spectroscopy demonstrates a typical, alpha + beta-fold found in many proteins with different functions. The, molecular surface of the protein reveals a small, highly acidic pocket, comprising loop B (Asp36, Asp37, Asp38), the end of beta2 (Glu39), and, loop D (Ser57, Ser58, Ser61), indicating that the protein would have a, possible cation binding site. The NMR resonances of several amino acids, within the acidic binding pocket in MTH1880, shifted upon addition of, calcium ion. This calcium binding motif and overall topology of MTH1880, differ from those of other calcium binding proteins. MTH1880 did not show, a calcium-induced conformational change typical of calcium sensor, proteins. Therefore, we propose that the MTH1880 protein contains a novel, motif for calcium-specific binding, and may function as a calcium, buffering protein.
About this Structure
1IQS is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
Reference
Solution structure of a novel calcium binding protein, MTH1880, from Methanobacterium thermoautotrophicum., Lee CH, Jung JW, Yee A, Arrowsmith CH, Lee W, Protein Sci. 2004 Apr;13(4):1148-54. PMID:15044740
Page seeded by OCA on Sat Nov 24 22:23:21 2007
