STRUCTURE AT PH 6.5 OF FERREDOXIN-I FROM AZOTOBACTER-VINELANDII AT 2.3 ANGSTROM RESOLUTION

被引:30
作者
MERRITT, EA [1 ]
STOUT, GH [1 ]
TURLEY, S [1 ]
SIEKER, LC [1 ]
JENSEN, LH [1 ]
ORMEJOHNSON, WH [1 ]
机构
[1] MIT,DEPT CHEM,CAMBRIDGE,MA 02139
来源
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY | 1993年 / 49卷
关键词
D O I
10.1107/S0907444992007248
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Ferredoxin I from Azotobacter vinelandii (AvFdI) is an iron-sulfur protein composed of 106 amino acids, seven Fe atoms and eight inorganic S* atoms. A crystallographic redetermination of its structure showed the originally reported structure to be incorrect. We report here the crystal structure of AvFdI at pH 6.5. Extensive refinement has led to a final R value of 0.170 for all 6986 non-extinct reflections in the range 10-2.3 angstrom using a solvent model which includes 98 discrete solvent atoms with occupancies between 0.3 and 1.0 and an average B value of 22.5 angstrom2. The first half of the peptide chain closely resembles that of the 55-residue ferredoxin from Peptococcus aerogenes (PaFd), while the remainder consists of three turns of helix and a series of loops which form a cap over part of the molecular core. Despite the similarities in structure and surroundings, the corresponding 4Fe4S* clusters in PaFd and AvFdI have strikingly different redox potentials; a possible explanation has been sought in the differing hydration models for the two molecules.
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页码:272 / 281
页数:10
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