1fer: Difference between revisions

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New page: left|200px<br /><applet load="1fer" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fer, resolution 2.3Å" /> '''STRUCTURE AT PH 6.5 O...
 
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[[Image:1fer.jpg|left|200px]]<br /><applet load="1fer" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fer.jpg|left|200px]]<br /><applet load="1fer" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fer, resolution 2.3&Aring;" />
caption="1fer, resolution 2.3&Aring;" />
'''STRUCTURE AT PH 6.5 OF FERREDOXIN I FROM AZOTOBACTER VINELANDII AT 2.3 ANGSTROMS RESOLUTION'''<br />
'''STRUCTURE AT PH 6.5 OF FERREDOXIN I FROM AZOTOBACTER VINELANDII AT 2.3 ANGSTROMS RESOLUTION'''<br />


==Overview==
==Overview==
Ferredoxin I from Azotobacter vinelandii (AvFdI) is an iron-sulfur protein, composed of 106 amino acids, seven Fe atoms and eight inorganic S* atoms., A crystallographic redetermination of its structure showed the originally, reported structure to be incorrect. We report here the crystal structure, of AvFdI at pH 6.5. Extensive refinement has led to a final R value of, 0.170 for all 6986 non-extinct reflections in the range 10-2.3 A using a, solvent model which includes 98 discrete solvent atoms with occupancies, between 0.3 and 1.0 and an average B value of 22.5 A(2). The first half of, the peptide chain closely resembles that of the 55-residue ferredoxin from, Peptococcus aerogenes (PaFd), while the remainder consists of three turns, of helix and a series of loops which form a cap over part of the molecular, core. Despite the similarities in structure and surroundings, the, corresponding 4Fe4S* clusters in PaFd and AvFdI have strikingly different, redox potentials; a possible explanation has been sought in the differing, hydration models for the two molecules.
Ferredoxin I from Azotobacter vinelandii (AvFdI) is an iron-sulfur protein composed of 106 amino acids, seven Fe atoms and eight inorganic S* atoms. A crystallographic redetermination of its structure showed the originally reported structure to be incorrect. We report here the crystal structure of AvFdI at pH 6.5. Extensive refinement has led to a final R value of 0.170 for all 6986 non-extinct reflections in the range 10-2.3 A using a solvent model which includes 98 discrete solvent atoms with occupancies between 0.3 and 1.0 and an average B value of 22.5 A(2). The first half of the peptide chain closely resembles that of the 55-residue ferredoxin from Peptococcus aerogenes (PaFd), while the remainder consists of three turns of helix and a series of loops which form a cap over part of the molecular core. Despite the similarities in structure and surroundings, the corresponding 4Fe4S* clusters in PaFd and AvFdI have strikingly different redox potentials; a possible explanation has been sought in the differing hydration models for the two molecules.


==About this Structure==
==About this Structure==
1FER 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 F3S and SF4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FER OCA].  
1FER 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=F3S:'>F3S</scene> and <scene name='pdbligand=SF4:'>SF4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FER OCA].  


==Reference==
==Reference==
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[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Jensen, L.H.]]
[[Category: Jensen, L H.]]
[[Category: Merritt, E.A.]]
[[Category: Merritt, E A.]]
[[Category: Orme-Johnson, W.H.]]
[[Category: Orme-Johnson, W H.]]
[[Category: Sieker, L.C.]]
[[Category: Sieker, L C.]]
[[Category: Stout, G.H.]]
[[Category: Stout, G H.]]
[[Category: Turley, S.]]
[[Category: Turley, S.]]
[[Category: F3S]]
[[Category: F3S]]
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[[Category: electron transfer(iron-sulfur protein)]]
[[Category: electron transfer(iron-sulfur protein)]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:51:38 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:37:54 2008''

Revision as of 13:37, 21 February 2008

File:1fer.jpg


1fer, resolution 2.3Å

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STRUCTURE AT PH 6.5 OF FERREDOXIN I FROM AZOTOBACTER VINELANDII AT 2.3 ANGSTROMS RESOLUTION

OverviewOverview

Ferredoxin I from Azotobacter vinelandii (AvFdI) is an iron-sulfur protein composed of 106 amino acids, seven Fe atoms and eight inorganic S* atoms. A crystallographic redetermination of its structure showed the originally reported structure to be incorrect. We report here the crystal structure of AvFdI at pH 6.5. Extensive refinement has led to a final R value of 0.170 for all 6986 non-extinct reflections in the range 10-2.3 A using a solvent model which includes 98 discrete solvent atoms with occupancies between 0.3 and 1.0 and an average B value of 22.5 A(2). The first half of the peptide chain closely resembles that of the 55-residue ferredoxin from Peptococcus aerogenes (PaFd), while the remainder consists of three turns of helix and a series of loops which form a cap over part of the molecular core. Despite the similarities in structure and surroundings, the corresponding 4Fe4S* clusters in PaFd and AvFdI have strikingly different redox potentials; a possible explanation has been sought in the differing hydration models for the two molecules.

About this StructureAbout this Structure

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

ReferenceReference

Structure at pH 6.5 of ferredoxin I from Azotobacter vinelandii at 2.3 A resolution., Merritt EA, Stout GH, Turley S, Sieker LC, Jehsen LH, Orme-Johnson WH, Acta Crystallogr D Biol Crystallogr. 1993 Mar 1;49(Pt 2):272-81. PMID:15299532

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