1fxa
From Proteopedia
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, resolution 2.5Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
CRYSTALLIZATION AND STRUCTURE DETERMINATION TO 2.5-ANGSTROMS RESOLUTION OF THE OXIDIZED [2FE-2S] FERREDOXIN ISOLATED FROM ANABAENA 7120
Overview
The molecular structure of the oxidized form of the [2Fe-2S] ferredoxin isolated from the cyanobacterium Anabaena species strain PCC 7120 has been determined by X-ray diffraction analysis to a nominal resolution of 2.5 A and refined to a crystallographic R factor of 18.7%. Crystals used in this investigation belong to the space group P2(1)2(1)2(1) with unit cell dimensions of a = 37.42 A, b = 38.12 A, and c = 147.12 A and two molecules in the asymmetric unit. The three-dimensional structure of this ferredoxin was solved by a method that combined X-ray data from one isomorphous heavy-atom derivative with noncrystallographic symmetry averaging and solvent flattening. As in other plant-type [2Fe-2S] ferredoxins, the iron-sulfur cluster is located toward the outer edge of the molecule, and the irons are tetrahedrally coordinated by both inorganic sulfurs and sulfurs provided by protein cysteine residues. The main secondary structural elements include four strands of beta-pleated sheet and three alpha-helical regions.
About this Structure
1FXA is a Single protein structure of sequence from Anabaena sp.. Full crystallographic information is available from OCA.
Reference
Crystallization and structure determination to 2.5-A resolution of the oxidized [2Fe-2S] ferredoxin isolated from Anabaena 7120., Rypniewski WR, Breiter DR, Benning MM, Wesenberg G, Oh BH, Markley JL, Rayment I, Holden HM, Biochemistry. 1991 Apr 30;30(17):4126-31. PMID:1902376
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