NDLI: Structure of the oxidized long-chain flavodoxin from Anabaena 7120 at 2 A resolution.

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Structure of the oxidized long-chain flavodoxin from Anabaena 7120 at 2 A resolution.

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Structure of the oxidized long-chain flavodoxin from Anabaena 7120 at 2 A resolution.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Rao, S. T. Satyshur, K. A. Stockman, B. J. Shaffie, F. Markley, J. L. Yu, C. Sundarlingam, M.
Description	Author Affiliation: Rao ST ( Department of Chemistry, Ohio State University, Columbus 43210.)
Abstract	The structure of the long-chain flavodoxin from the photosynthetic cyanobacterium Anabaena 7120 has been determined at 2 A 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 P2(1) with a = 48.0, b = 32.0, c = 51.6 A, and beta = 92 degrees, and one molecule in the asymmetric unit. The 2 A 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 > 2 sigma 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 A and 3.5 A, respectively, whereas in the third flavodoxin the distance is 3.1 A, 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.(ABSTRACT TRUNCATED AT 400 WORDS)
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	11
Volume Number	1
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	1992-11-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Anabaena Metabolism Flavodoxin Chemistry Protein Structure, Secondary Protein Structure, Tertiary Amino Acid Sequence Flavin Mononucleotide Models, Molecular Molecular Sequence Data Sequence Homology, Amino Acid Thermodynamics X-ray Diffraction Comparative Study Research Support, Non-u.s. Gov't Research Support, U.s. Gov't, Non-p.h.s. Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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