1hrq: Difference between revisions

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New page: left|200px<br /><applet load="1hrq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hrq" /> '''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF ...
 
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[[Image:1hrq.jpg|left|200px]]<br /><applet load="1hrq" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1hrq.jpg|left|200px]]<br /><applet load="1hrq" size="350" color="white" frame="true" align="right" spinBox="true"  
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'''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR'''<br />
'''THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR'''<br />


==Overview==
==Overview==
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.
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==
1HRQ 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=1HRQ OCA].  
1HRQ 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=1HRQ OCA].  


==Reference==
==Reference==
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[[Category: Bertini, I.]]
[[Category: Bertini, I.]]
[[Category: Dikiy, A.]]
[[Category: Dikiy, A.]]
[[Category: Kastrau, D.H.W.]]
[[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 protein)]]
[[Category: electron transfer (iron-sulfur protein)]]


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Revision as of 14:04, 21 February 2008

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1hrq

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THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE REDUCED HIGH-POTENTIAL IRON-SULFUR PROTEIN FROM CHROMATIUM VINOSUM THROUGH NMR

OverviewOverview

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 StructureAbout this Structure

1HRQ is a Single protein structure of sequence from Allochromatium vinosum with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

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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