FEBS Letters | |
The crystal structure of the three‐iron ferredoxin II from Desulfovibrio gigas | |
Adman, E.T.1  LeGall, J.2  Jensen, L.H.1  Sieker, L.C.1  Kissinger, C.R.1  | |
[1]Department of Biological Structure, University of Washington, Seattle, WA 98195 USA | |
[2]Department of Biochemistry, University of Georgia, Athens, GA 30602, USA | |
关键词: Ferredoxin; Iron-sulfur cluster; Crystal structure; Anomalous scattering; Disulfide bridge; (Desulfovibrio gigas); | |
DOI : 10.1016/0014-5793(89)80580-0 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
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【 摘 要 】
The crystal structure of oxidized ferredoxin II from the sulfate-reducing bacterium Desulfovibrio gigas has been determined and refined at 1.7 Å resolution. The folding of the polypeptide chain is similar to that of the 2[4Fe-4S] ferredoxin in Peptococcus aerogenes, except for an extended helical segment near the C-terminus. The single [3Fe-4S] cluster in D. gigas is similar to a [4Fe-4S] cluster, but lacks one Fe atom and is coordinated to Cys-8, -14 and -50. The side chain of Cys-11 is not bound to the cluster, but is rotated toward the solvent and modified by some, as yet undetermined, chemical group. Cys-18 and Cys-42 form a disulfide bridge. A previously undetected extra amino acid is found after residue 55.
【 授权许可】
Unknown
【 预 览 】
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RO201912020291695ZK.pdf | 301KB | ![]() |