1f37

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(New page: 200px<br /><applet load="1f37" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f37, resolution 2.3&Aring;" /> '''STRUCTURE OF A THIORE...)
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[[Image:1f37.jpg|left|200px]]<br /><applet load="1f37" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1f37, resolution 2.3&Aring;" />
caption="1f37, resolution 2.3&Aring;" />
'''STRUCTURE OF A THIOREDOXIN-LIKE [2FE-2S] FERREDOXIN FROM AQUIFEX AEOLICUS'''<br />
'''STRUCTURE OF A THIOREDOXIN-LIKE [2FE-2S] FERREDOXIN FROM AQUIFEX AEOLICUS'''<br />
==Overview==
==Overview==
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The 2.3 A resolution crystal structure of a [2Fe-2S] cluster containing, ferredoxin from Aquifex aeolicus reveals a thioredoxin-like fold that is, novel among iron-sulfur proteins. The [2Fe-2S] cluster is located near the, surface of the protein, at a site corresponding to that of the active-site, disulfide bridge in thioredoxin. The four cysteine ligands are located, near the ends of two surface loops. Two of these ligands can be, substituted by non-native cysteine residues introduced throughout a, stretch of the polypeptide chain that forms a protruding loop extending, away from the cluster. The presence of homologs of this ferredoxin as, components of more complex anaerobic and aerobic electron transfer systems, indicates that this is a versatile fold for biological redox processes.
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The 2.3 A resolution crystal structure of a [2Fe-2S] cluster containing ferredoxin from Aquifex aeolicus reveals a thioredoxin-like fold that is novel among iron-sulfur proteins. The [2Fe-2S] cluster is located near the surface of the protein, at a site corresponding to that of the active-site disulfide bridge in thioredoxin. The four cysteine ligands are located near the ends of two surface loops. Two of these ligands can be substituted by non-native cysteine residues introduced throughout a stretch of the polypeptide chain that forms a protruding loop extending away from the cluster. The presence of homologs of this ferredoxin as components of more complex anaerobic and aerobic electron transfer systems indicates that this is a versatile fold for biological redox processes.
==About this Structure==
==About this Structure==
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1F37 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with FES and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F37 OCA].
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1F37 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=FES:'>FES</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F37 OCA].
==Reference==
==Reference==
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[[Category: Kuhn, P.]]
[[Category: Kuhn, P.]]
[[Category: Meyer, J.]]
[[Category: Meyer, J.]]
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[[Category: Rees, D.C.]]
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[[Category: Rees, D C.]]
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[[Category: Soltis, S.M.]]
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[[Category: Soltis, S M.]]
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[[Category: Yeh, A.P.]]
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[[Category: Yeh, A P.]]
[[Category: FES]]
[[Category: FES]]
[[Category: GOL]]
[[Category: GOL]]
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[[Category: thioredoxin fold]]
[[Category: thioredoxin fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:34:15 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:20 2008''

Revision as of 10:34, 21 February 2008


1f37, resolution 2.3Å

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STRUCTURE OF A THIOREDOXIN-LIKE [2FE-2S] FERREDOXIN FROM AQUIFEX AEOLICUS

Overview

The 2.3 A resolution crystal structure of a [2Fe-2S] cluster containing ferredoxin from Aquifex aeolicus reveals a thioredoxin-like fold that is novel among iron-sulfur proteins. The [2Fe-2S] cluster is located near the surface of the protein, at a site corresponding to that of the active-site disulfide bridge in thioredoxin. The four cysteine ligands are located near the ends of two surface loops. Two of these ligands can be substituted by non-native cysteine residues introduced throughout a stretch of the polypeptide chain that forms a protruding loop extending away from the cluster. The presence of homologs of this ferredoxin as components of more complex anaerobic and aerobic electron transfer systems indicates that this is a versatile fold for biological redox processes.

About this Structure

1F37 is a Single protein structure of sequence from Aquifex aeolicus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of a thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus., Yeh AP, Chatelet C, Soltis SM, Kuhn P, Meyer J, Rees DC, J Mol Biol. 2000 Jul 14;300(3):587-95. PMID:10884354[[Category: [2fe-2s] cluster]]

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