1uwm
From Proteopedia
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| - | [[Image:1uwm.gif|left|200px]] | + | [[Image:1uwm.gif|left|200px]] |
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| - | '''REDUCED FERREDOXIN 6 FROM RHODOBACTER CAPSULATUS''' | + | {{Structure |
| + | |PDB= 1uwm |SIZE=350|CAPTION= <scene name='initialview01'>1uwm</scene>, resolution 2.00Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Fes+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''REDUCED FERREDOXIN 6 FROM RHODOBACTER CAPSULATUS''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UWM is a [ | + | 1UWM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodobacter_capsulatus Rhodobacter capsulatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UWM OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of a [2Fe-2S] ferredoxin from Rhodobacter capsulatus likely involved in Fe-S cluster biogenesis and conformational changes observed upon reduction., Sainz G, Jakoncic J, Sieker LC, Stojanoff V, Sanishvili N, Asso M, Bertrand P, Armengaud J, Jouanneau Y, J Biol Inorg Chem. 2006 Mar;11(2):235-46. Epub 2006 Jan 10. PMID:[http:// | + | Structure of a [2Fe-2S] ferredoxin from Rhodobacter capsulatus likely involved in Fe-S cluster biogenesis and conformational changes observed upon reduction., Sainz G, Jakoncic J, Sieker LC, Stojanoff V, Sanishvili N, Asso M, Bertrand P, Armengaud J, Jouanneau Y, J Biol Inorg Chem. 2006 Mar;11(2):235-46. Epub 2006 Jan 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16402206 16402206] |
[[Category: Rhodobacter capsulatus]] | [[Category: Rhodobacter capsulatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Stojanoff, V.]] | [[Category: Stojanoff, V.]] | ||
[[Category: FES]] | [[Category: FES]] | ||
| - | [[Category: 2fe- | + | [[Category: 2fe-2]] |
[[Category: electron transport]] | [[Category: electron transport]] | ||
[[Category: ferredoxin]] | [[Category: ferredoxin]] | ||
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[[Category: metal-binding]] | [[Category: metal-binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:37:45 2008'' |
Revision as of 12:37, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
REDUCED FERREDOXIN 6 FROM RHODOBACTER CAPSULATUS
Overview
FdVI from Rhodobacter capsulatus is structurally related to a group of [2Fe-2S] ferredoxins involved in iron-sulfur cluster biosynthesis. Comparative genomics suggested that FdVI and orthologs found in alpha-Proteobacteria are involved in this process. Here, the crystal structure of FdVI has been determined for both the oxidized and the reduced protein. The [2Fe-2S] cluster lies 6 A below the protein surface in a hydrophobic pocket without access to the solvent. This particular cluster environment might explain why the FdVI midpoint redox potential (-306 mV at pH 8.0) did not show temperature or ionic strength dependence. Besides the four cysteines that bind the cluster, FdVI features an extra cysteine which is located close to the S1 atom of the cluster and is oriented in a position such that its thiol group points towards the solvent. Upon reduction, the general fold of the polypeptide chain was almost unchanged. The [2Fe-2S] cluster underwent a conformational change from a planar to a distorted lozenge. In the vicinity of the cluster, the side chain of Met24 was rotated by 180 degrees , bringing its S atom within hydrogen-bonding distance of the S2 atom of the cluster. The reduced molecule also featured a higher content of bound water molecules, and more extensive hydrogen-bonding networks compared with the oxidized molecule. The unique conformational changes observed in FdVI upon reduction are discussed in the light of structural studies performed on related ferredoxins.
About this Structure
1UWM is a Single protein structure of sequence from Rhodobacter capsulatus. Full crystallographic information is available from OCA.
Reference
Structure of a [2Fe-2S] ferredoxin from Rhodobacter capsulatus likely involved in Fe-S cluster biogenesis and conformational changes observed upon reduction., Sainz G, Jakoncic J, Sieker LC, Stojanoff V, Sanishvili N, Asso M, Bertrand P, Armengaud J, Jouanneau Y, J Biol Inorg Chem. 2006 Mar;11(2):235-46. Epub 2006 Jan 10. PMID:16402206
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