1nip

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(New page: 200px<br /><applet load="1nip" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nip, resolution 2.9&Aring;" /> '''CRYSTALLOGRAPHIC STRU...)
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caption="1nip, resolution 2.9&Aring;" />
'''CRYSTALLOGRAPHIC STRUCTURE OF THE NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII'''<br />
'''CRYSTALLOGRAPHIC STRUCTURE OF THE NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII'''<br />
==Overview==
==Overview==
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The nitrogenase enzyme system catalyzes the ATP (adenosine, triphosphate)-dependent reduction of dinitrogen to ammonia during the, process of nitrogen fixation. Nitrogenase consists of two proteins: the, iron (Fe)-protein, which couples hydrolysis of ATP to electron transfer, and the molybdenum-iron (MoFe)-protein, which contains the dinitrogen, binding site. In order to address the role of ATP in nitrogen fixation, the crystal structure of the nitrogenase Fe-protein from Azotobacter, vinelandii has been determined at 2.9 angstrom (A) resolution. Fe-protein, is a dimer of two identical subunits that coordinate a single 4Fe:4S, cluster. Each subunit folds as a single alpha/beta type domain, which, together symmetrically ligate the surface exposed 4Fe:4S cluster through, two cysteines from each subunit. A single bound ADP (adenosine, diphosphate) molecule is located in the interface region between the two, subunits. Because the phosphate groups of this nucleotide are, approximately 20 A from the 4Fe:4S cluster, it is unlikely that ATP, hydrolysis and electron transfer are directly coupled. Instead, it appears, that interactions between the nucleotide and cluster sites must be, indirectly coupled by allosteric changes occurring at the subunit, interface. The coupling between protein conformation and nucleotide, hydrolysis in Fe-protein exhibits general similarities to the H-Ras p21, and recA proteins that have been recently characterized structurally. The, Fe-protein structure may be relevant to the functioning of other, biochemical energy-transducing systems containing two nucleotide-binding, sites, including membrane transport proteins.
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The nitrogenase enzyme system catalyzes the ATP (adenosine triphosphate)-dependent reduction of dinitrogen to ammonia during the process of nitrogen fixation. Nitrogenase consists of two proteins: the iron (Fe)-protein, which couples hydrolysis of ATP to electron transfer, and the molybdenum-iron (MoFe)-protein, which contains the dinitrogen binding site. In order to address the role of ATP in nitrogen fixation, the crystal structure of the nitrogenase Fe-protein from Azotobacter vinelandii has been determined at 2.9 angstrom (A) resolution. Fe-protein is a dimer of two identical subunits that coordinate a single 4Fe:4S cluster. Each subunit folds as a single alpha/beta type domain, which together symmetrically ligate the surface exposed 4Fe:4S cluster through two cysteines from each subunit. A single bound ADP (adenosine diphosphate) molecule is located in the interface region between the two subunits. Because the phosphate groups of this nucleotide are approximately 20 A from the 4Fe:4S cluster, it is unlikely that ATP hydrolysis and electron transfer are directly coupled. Instead, it appears that interactions between the nucleotide and cluster sites must be indirectly coupled by allosteric changes occurring at the subunit interface. The coupling between protein conformation and nucleotide hydrolysis in Fe-protein exhibits general similarities to the H-Ras p21 and recA proteins that have been recently characterized structurally. The Fe-protein structure may be relevant to the functioning of other biochemical energy-transducing systems containing two nucleotide-binding sites, including membrane transport proteins.
==About this Structure==
==About this Structure==
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1NIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with MG, SF4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NIP OCA].
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1NIP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NIP OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Chakrabarti, P.]]
[[Category: Chakrabarti, P.]]
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[[Category: Georgiadis, M.M.]]
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[[Category: Georgiadis, M M.]]
[[Category: Komiya, H.]]
[[Category: Komiya, H.]]
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[[Category: Kornuc, J.J.]]
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[[Category: Kornuc, J J.]]
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[[Category: Rees, D.C.]]
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[[Category: Rees, D C.]]
[[Category: Woo, D.]]
[[Category: Woo, D.]]
[[Category: ADP]]
[[Category: ADP]]
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[[Category: iron protein]]
[[Category: iron protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:17:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:06:31 2008''

Revision as of 12:06, 21 February 2008

Image:1nip.gif

1nip, resolution 2.9Å

Drag the structure with the mouse to rotate

CRYSTALLOGRAPHIC STRUCTURE OF THE NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII

Overview

The nitrogenase enzyme system catalyzes the ATP (adenosine triphosphate)-dependent reduction of dinitrogen to ammonia during the process of nitrogen fixation. Nitrogenase consists of two proteins: the iron (Fe)-protein, which couples hydrolysis of ATP to electron transfer, and the molybdenum-iron (MoFe)-protein, which contains the dinitrogen binding site. In order to address the role of ATP in nitrogen fixation, the crystal structure of the nitrogenase Fe-protein from Azotobacter vinelandii has been determined at 2.9 angstrom (A) resolution. Fe-protein is a dimer of two identical subunits that coordinate a single 4Fe:4S cluster. Each subunit folds as a single alpha/beta type domain, which together symmetrically ligate the surface exposed 4Fe:4S cluster through two cysteines from each subunit. A single bound ADP (adenosine diphosphate) molecule is located in the interface region between the two subunits. Because the phosphate groups of this nucleotide are approximately 20 A from the 4Fe:4S cluster, it is unlikely that ATP hydrolysis and electron transfer are directly coupled. Instead, it appears that interactions between the nucleotide and cluster sites must be indirectly coupled by allosteric changes occurring at the subunit interface. The coupling between protein conformation and nucleotide hydrolysis in Fe-protein exhibits general similarities to the H-Ras p21 and recA proteins that have been recently characterized structurally. The Fe-protein structure may be relevant to the functioning of other biochemical energy-transducing systems containing two nucleotide-binding sites, including membrane transport proteins.

About this Structure

1NIP is a Single protein structure of sequence from Azotobacter vinelandii with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystallographic structure of the nitrogenase iron protein from Azotobacter vinelandii., Georgiadis MM, Komiya H, Chakrabarti P, Woo D, Kornuc JJ, Rees DC, Science. 1992 Sep 18;257(5077):1653-9. PMID:1529353

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