Structure of the oxidized long‐chain flavodoxin from anabaena 7120 at 2 å resolution

The structure of the long‐chain flavodoxin from the photosynthetic cyanobacterium Anabaena 7120 has been determined at 2 å resolution by the molecular replacement method using the atomic coordinates of the long‐chain flavodoxin from Anacystis nidulans. The structure of a third long‐chain flavodoxin...

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Bibliographic Details
Published in:Protein science 1992-11, Vol.1 (11), p.1413-1427
Main Authors: Rao, S. T., Shaffie, Fathieh, Yu, Carlos, Satyshur, Kenneth A., Stockman, Brian J., Markley, John L., Sundaralingam, M.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Anabaena - metabolism
Anabaena 7120
Flavin Mononucleotide - metabolism
Flavodoxin - chemistry
Flavodoxin - metabolism
long‐chain flavodoxin
Models, Molecular
Molecular Sequence Data
oxidation
Protein Structure, Secondary
Protein Structure, Tertiary
Sequence Homology, Amino Acid
Thermodynamics
X-Ray Diffraction
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Summary:The structure of the long‐chain flavodoxin from the photosynthetic cyanobacterium Anabaena 7120 has been determined at 2 å resolution by the molecular replacement method using the atomic coordinates of the long‐chain flavodoxin from Anacystis nidulans. The structure of a third long‐chain flavodoxin from Chondrus crispus has recently been reported. Crystals of oxidized A. 7120 flavodoxin belong to the monoclinic space group P21 with a = 48.0, b = 32.0, c = 51.6 å, and β = 92°, and one molecule in the asymmetric unit. The 2 å intensity data were collected with oscillation films at the CHESS synchrotron source and processed to yield 9,795 independent intensities with Rmerg of 0.07. Of these, 8,493 reflections had I > 2σ and were used in the analysis. The model obtained by molecular replacement was initially refined by simulated annealing using the XPLOR program. Repeated refitting into omit maps and several rounds of conjugate gradient refinement led to an R‐value of 0.185 for a model containing atoms for protein residues 2–169, flavin mononucleotide (FMN), and 104 solvent molecules. The FMN shows many interactions with the protein with the isoalloxazine ring, ribityl sugar, and the 5′‐phosphate. The flavin ring has its pyrimidine end buried into the protein, and the functional dimethyl benzene edge is accessible to solvent. The FMN interactions in all three long‐chain structures are similar except for the O4′ of the ribityl chain, which interacts with the hydroxyl group of Thr 88 side chain in A. 7120, while with a water molecule in the other two. The phosphate group interacts with the atoms of the 9–15 loop as well as with NE1 of Trp 57. The N5 atom of flavin interacts with the amide NH of Ile 59 in A. 7120, whereas in A. nidulans it interacts with the amide NH of Val 59 in a similar manner. In C. crispus flavodoxin, N5 forms a hydrogen bond with the side chain hydroxyl group of the equivalent Thr 58. The hydrogen bond distances to the backbone NH groups in the first two flavodoxins are 3.6 å and 3.5 å, respectively, whereas in the third flavodoxin the distance is 3.1 å, close to the normal value. Even though the hydrogen bond distances are long in the first two cases, still they might have significant energy because their microenvironment in the protein is not accessible to solvent. In all three long‐chain flavodoxins, a water molecule bridges the ends of the inserted loop in the β5 strand and minimally perturbs its hydrogen bonding with β4. Many of the wa
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.5560011103