1m60

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(New page: 200px<br /><applet load="1m60" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m60" /> '''Solution Structure of Zinc-substituted cytoc...)
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'''Solution Structure of Zinc-substituted cytochrome c'''<br />
'''Solution Structure of Zinc-substituted cytochrome c'''<br />
==Overview==
==Overview==
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Zinc-substituted cytochrome c has been widely used in studies of, protein-protein interactions and photo-induced electron transfer reactions, between proteins. However, the coordination geometry of zinc in, zinc-substituted cyt c has not yet been determined; two different opinions, about the coordination have been reached. Here the solution structures of, zinc-substituted cytochrome c that might be five-coordinated and, six-coordinated have been refined separately by using (1)H NMR, spectroscopy, and the zinc coordination geometry was determined just by, NOE distance constraints. Structural analysis of the energy-minimized, average solution structures of both the pentacoordinated and, hexacoordinated geometries indicate that that zinc in zinc-substituted cyt, c should be bound to both His18 and Met80, which means that the zinc is, six-coordinated. RMSD values of the family of 25 six-coordinated, structures from the average structure are 0.66+/-0.13 A and 1.09+/-0.16 A, for the backbone and all heavy atoms, respectively. A statistical analysis, of the structure indicates its satisfactory quality. Comparison of the, solution structure of the six-coordinated energy-minimized average, structure of zinc-substituted cytochrome c with the solution structure of, reduced cytochrome c reveals that for the overall folding the secondary, structure elements are very close. The availability of the structure, provides for a better understanding of the protein-protein complex and for, electron transfer processes between Zn cyt c and other metalloproteins.
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Zinc-substituted cytochrome c has been widely used in studies of protein-protein interactions and photo-induced electron transfer reactions between proteins. However, the coordination geometry of zinc in zinc-substituted cyt c has not yet been determined; two different opinions about the coordination have been reached. Here the solution structures of zinc-substituted cytochrome c that might be five-coordinated and six-coordinated have been refined separately by using (1)H NMR spectroscopy, and the zinc coordination geometry was determined just by NOE distance constraints. Structural analysis of the energy-minimized average solution structures of both the pentacoordinated and hexacoordinated geometries indicate that that zinc in zinc-substituted cyt c should be bound to both His18 and Met80, which means that the zinc is six-coordinated. RMSD values of the family of 25 six-coordinated structures from the average structure are 0.66+/-0.13 A and 1.09+/-0.16 A for the backbone and all heavy atoms, respectively. A statistical analysis of the structure indicates its satisfactory quality. Comparison of the solution structure of the six-coordinated energy-minimized average structure of zinc-substituted cytochrome c with the solution structure of reduced cytochrome c reveals that for the overall folding the secondary structure elements are very close. The availability of the structure provides for a better understanding of the protein-protein complex and for electron transfer processes between Zn cyt c and other metalloproteins.
==About this Structure==
==About this Structure==
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1M60 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with HES as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M60 OCA].
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1M60 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=HES:'>HES</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M60 OCA].
==Reference==
==Reference==
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[[Category: six-coordinated zinc cyt c]]
[[Category: six-coordinated zinc cyt c]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:10:25 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:54 2008''

Revision as of 11:51, 21 February 2008


1m60

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Solution Structure of Zinc-substituted cytochrome c

Overview

Zinc-substituted cytochrome c has been widely used in studies of protein-protein interactions and photo-induced electron transfer reactions between proteins. However, the coordination geometry of zinc in zinc-substituted cyt c has not yet been determined; two different opinions about the coordination have been reached. Here the solution structures of zinc-substituted cytochrome c that might be five-coordinated and six-coordinated have been refined separately by using (1)H NMR spectroscopy, and the zinc coordination geometry was determined just by NOE distance constraints. Structural analysis of the energy-minimized average solution structures of both the pentacoordinated and hexacoordinated geometries indicate that that zinc in zinc-substituted cyt c should be bound to both His18 and Met80, which means that the zinc is six-coordinated. RMSD values of the family of 25 six-coordinated structures from the average structure are 0.66+/-0.13 A and 1.09+/-0.16 A for the backbone and all heavy atoms, respectively. A statistical analysis of the structure indicates its satisfactory quality. Comparison of the solution structure of the six-coordinated energy-minimized average structure of zinc-substituted cytochrome c with the solution structure of reduced cytochrome c reveals that for the overall folding the secondary structure elements are very close. The availability of the structure provides for a better understanding of the protein-protein complex and for electron transfer processes between Zn cyt c and other metalloproteins.

About this Structure

1M60 is a Single protein structure of sequence from Equus caballus with as ligand. Full crystallographic information is available from OCA.

Reference

Structural analysis of zinc-substituted cytochrome c., Qian C, Yao Y, Tong Y, Wang J, Tang W, J Biol Inorg Chem. 2003 Apr;8(4):394-400. Epub 2002 Dec 14. PMID:12761660

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