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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[[Image:1hrr.jpg|left|200px]]<br /><applet load="1hrr" size="350" color="white" frame="true" align="right" spinBox="true"
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'''THE THREE DIMENSIONAL STRUCTURE OF THE REDUCED HIGH POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR'''<br />
'''THE THREE DIMENSIONAL STRUCTURE OF THE REDUCED HIGH POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR'''<br />
==Overview==
==Overview==
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The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum, available in the literature [Gaillard, J., Albrand, J.-P., Moulis, J.-M., &amp; 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.
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The 1H NMR assignment of the reduced HiPIP from Chromatium vinosum available in the literature [Gaillard, J., Albrand, J.-P., Moulis, J.-M., &amp; 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==
==About this Structure==
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1HRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum] with SF4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HRR OCA].
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1HRR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Allochromatium_vinosum Allochromatium vinosum] with <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HRR OCA].
==Reference==
==Reference==
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[[Category: Bertini, I.]]
[[Category: Bertini, I.]]
[[Category: Dikiy, A.]]
[[Category: Dikiy, A.]]
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[[Category: Kastrau, D.H.W.]]
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[[Category: Kastrau, D H.W.]]
[[Category: Luchinat, C.]]
[[Category: Luchinat, C.]]
[[Category: Sompornpisut, P.]]
[[Category: Sompornpisut, P.]]
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[[Category: electron transfer (iron-sulfur)]]
[[Category: electron transfer (iron-sulfur)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:47:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:19 2008''

Revision as of 11:04, 21 February 2008


1hrr

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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 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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