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1f37
From Proteopedia
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|PDB= 1f37 |SIZE=350|CAPTION= <scene name='initialview01'>1f37</scene>, resolution 2.3Å | |PDB= 1f37 |SIZE=350|CAPTION= <scene name='initialview01'>1f37</scene>, resolution 2.3Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene> | + | |LIGAND= <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f37 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f37 OCA], [http://www.ebi.ac.uk/pdbsum/1f37 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f37 RCSB]</span> | ||
}} | }} | ||
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[[Category: Soltis, S M.]] | [[Category: Soltis, S M.]] | ||
[[Category: Yeh, A P.]] | [[Category: Yeh, A P.]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: GOL]] | ||
[[Category: [2fe-2s] cluster]] | [[Category: [2fe-2s] cluster]] | ||
[[Category: ferredoxin]] | [[Category: ferredoxin]] | ||
[[Category: thioredoxin fold]] | [[Category: thioredoxin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:14:56 2008'' |
Revision as of 17:15, 30 March 2008
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| , resolution 2.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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]]
Page seeded by OCA on Sun Mar 30 20:14:56 2008
