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BMC Struct Biol. 2006 Apr 9;6:8.

A tale of two ferredoxins: sequence similarity and structural differences.

Author information

1
Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390-9050, USA. krishna@sdsc.edu

Abstract

BACKGROUND:

Sequence similarity between proteins is usually considered a reliable indicator of homology. Pyruvate-ferredoxin oxidoreductase and quinol-fumarate reductase contain ferredoxin domains that bind [Fe-S] clusters and are involved in electron transport. Profile-based methods for sequence comparison, such as PSI-BLAST and HMMer, suggest statistically significant similarity between these domains.

RESULTS:

The sequence similarity between these ferredoxin domains resides in the area of the [Fe-S] cluster-binding sites. Although overall folds of these ferredoxins bear no obvious similarity, the regions of sequence similarity display a remarkable local structural similarity. These short regions with pronounced sequence motifs are incorporated in completely different structural environments. In pyruvate-ferredoxin oxidoreductase (bacterial ferredoxin), the hydrophobic core of the domain is completed by two beta-hairpins, whereas in quinol-fumarate reductase (alpha-helical ferredoxin), the cluster-binding motifs are part of a larger all-alpha-helical globin-like fold core.

CONCLUSION:

Functionally meaningful sequence similarity may sometimes be reflected only in local structural similarity, but not in global fold similarity. If detected and used naively, such similarities may lead to incorrect fold predictions.

PMID:
16603087
PMCID:
PMC1459171
DOI:
10.1186/1472-6807-6-8
[Indexed for MEDLINE]
Free PMC Article

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