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1YKG

Solution structure of the flavodoxin-like domain from the Escherichia coli sulfite reductase

Summary for 1YKG
Entry DOI10.2210/pdb1ykg/pdb
DescriptorSulfite reductase [NADPH] flavoprotein alpha-component, FLAVIN MONONUCLEOTIDE (2 entities in total)
Functional Keywordsflavoprotein, electron transport
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight18347.55
Authors
Sibille, N.,Blackledge, M.,Brutscher, B.,Coves, J.,Bersch, B. (deposition date: 2005-01-18, release date: 2005-07-05, Last modification date: 2024-05-29)
Primary citationSibille, N.,Blackledge, M.,Brutscher, B.,Coves, J.,Bersch, B.
Solution Structure of the Sulfite Reductase Flavodoxin-like Domain from Escherichia coli
Biochemistry, 44:9086-9095, 2005
Cited by
PubMed Abstract: The flavoprotein moiety of Escherichia coli sulfite reductase (SiR-FP) is homologous to electron transfer proteins such as cytochrome-P450 reductase (CPR) or nitric oxide synthase (NOS). We report on the three-dimensional structure of SiR-FP18, the flavodoxin-like domain of SiR-FP, which has been determined by NMR. In the holoenzyme, this domain plays an important role by shuttling electrons from the FAD to the hemoprotein (the beta-subunit). The structure presented here was determined using distance and torsion angle information in combination with residual dipolar couplings determined in two different alignment media. Several protein-FMN NOEs allowed us to place the prosthetic group in its binding pocket. The structure is well-resolved, and (15)N relaxation data indicate that SiR-FP18 is a compact domain. The binding interface with cytochrome c, a nonphysiological electron acceptor, has been determined using chemical shift mapping. Comparison of the SiR-FP18 structure with the corresponding domains from CPR and NOS shows that the fold of the protein core is highly conserved, but the analysis of the electrostatic surfaces reveals significant differences between the three domains. These observations are placed in the physiological context so they can contribute to the understanding of the electron transfer mechanism in the SiR holoenzyme.
PubMed: 15966732
DOI: 10.1021/bi050437p
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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