1g5p

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(New page: 200px<br /><applet load="1g5p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g5p, resolution 2.2&Aring;" /> '''NITROGENASE IRON PROT...)
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[[Image:1g5p.jpg|left|200px]]<br /><applet load="1g5p" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1g5p.jpg|left|200px]]<br /><applet load="1g5p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g5p, resolution 2.2&Aring;" />
caption="1g5p, resolution 2.2&Aring;" />
'''NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII'''<br />
'''NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII'''<br />
==Overview==
==Overview==
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The structure of the nitrogenase iron protein from Azotobacter vinelandii, in the all-ferrous [4Fe-4S](0) form has been determined to 2.25 A, resolution by using the multiwavelength anomalous diffraction (MAD), phasing technique. The structure demonstrates that major conformational, changes are not necessary either in the iron protein or in the cluster to, accommodate cluster reduction to the [4Fe-4S](0) oxidation state. A survey, of [4Fe-4S] clusters coordinated by four cysteine ligands in proteins of, known structure reveals that the [4Fe-4S] cluster of the iron protein has, the largest accessible surface area, suggesting that solvent exposure may, be relevant to the ability of the iron protein to exist in three oxidation, states.
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The structure of the nitrogenase iron protein from Azotobacter vinelandii in the all-ferrous [4Fe-4S](0) form has been determined to 2.25 A resolution by using the multiwavelength anomalous diffraction (MAD) phasing technique. The structure demonstrates that major conformational changes are not necessary either in the iron protein or in the cluster to accommodate cluster reduction to the [4Fe-4S](0) oxidation state. A survey of [4Fe-4S] clusters coordinated by four cysteine ligands in proteins of known structure reveals that the [4Fe-4S] cluster of the iron protein has the largest accessible surface area, suggesting that solvent exposure may be relevant to the ability of the iron protein to exist in three oxidation states.
==About this Structure==
==About this Structure==
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1G5P 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 SF4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G5P OCA].
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1G5P 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=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G5P OCA].
==Reference==
==Reference==
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[[Category: Nitrogenase]]
[[Category: Nitrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Angove, H.C.]]
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[[Category: Angove, H C.]]
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[[Category: Burgess, B.K.]]
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[[Category: Burgess, B K.]]
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[[Category: Chiu, H.J.]]
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[[Category: Chiu, H J.]]
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[[Category: Rees, D.C.]]
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[[Category: Rees, D C.]]
[[Category: Strop, P.]]
[[Category: Strop, P.]]
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[[Category: Takahara, P.M.]]
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[[Category: Takahara, P M.]]
[[Category: SF4]]
[[Category: SF4]]
[[Category: iron protein]]
[[Category: iron protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:43:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:23 2008''

Revision as of 10:46, 21 February 2008


1g5p, resolution 2.2Å

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NITROGENASE IRON PROTEIN FROM AZOTOBACTER VINELANDII

Overview

The structure of the nitrogenase iron protein from Azotobacter vinelandii in the all-ferrous [4Fe-4S](0) form has been determined to 2.25 A resolution by using the multiwavelength anomalous diffraction (MAD) phasing technique. The structure demonstrates that major conformational changes are not necessary either in the iron protein or in the cluster to accommodate cluster reduction to the [4Fe-4S](0) oxidation state. A survey of [4Fe-4S] clusters coordinated by four cysteine ligands in proteins of known structure reveals that the [4Fe-4S] cluster of the iron protein has the largest accessible surface area, suggesting that solvent exposure may be relevant to the ability of the iron protein to exist in three oxidation states.

About this Structure

1G5P is a Single protein structure of sequence from Azotobacter vinelandii with as ligand. Active as Nitrogenase, with EC number 1.18.6.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of the all-ferrous [4Fe-4S]0 form of the nitrogenase iron protein from Azotobacter vinelandii., Strop P, Takahara PM, Chiu H, Angove HC, Burgess BK, Rees DC, Biochemistry. 2001 Jan 23;40(3):651-6. PMID:11170381

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