1hrr
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(New page: 200px<br /><applet load="1hrr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hrr" /> '''THE THREE DIMENSIONAL STRUCTURE OF THE REDUC...)
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Revision as of 14:40, 20 November 2007
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THE THREE DIMENSIONAL STRUCTURE OF THE REDUCED HIGH POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR
Overview
The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum, available in the literature [Gaillard, J., Albrand, J.-P., Moulis, J.-M., & Wemmer, D. E. (1992) Biochemistry 31, 5632-5639] has been extended up to, 85% of the total protein protons. Ninety percent of the nitrogens have, been assigned. Then the solution structure has been obtained using as many, as 1147 meaningful NOE connectivities. The protein is sizably paramagnetic, even though the ground state is a singlet. Nevertheless, the final RMSD, values are 0.62 and 1.19 A for the backbone and the heavy atoms, respectively. These values compare well with those for diamagnetic, proteins of the same size. The solution structure is discussed in the, light of the available structural information from X-ray data.
About this Structure
1HRR is a Single protein structure of sequence from Allochromatium vinosum with SF4 as ligand. Full crystallographic information is available from OCA.
Reference
The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR., Banci L, Bertini I, Dikiy A, Kastrau DH, Luchinat C, Sompornpisut P, Biochemistry. 1995 Jan 10;34(1):206-19. PMID:7819198
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