H
IPR015915

Kelch-type beta propeller

InterPro entry
Short nameKelch-typ_b-propeller
Overlapping entries
 
BTB-kelch protein (IPR017096)

Description

This entry represents the 6-bladed Kelch β-propeller, which consists of six 4-stranded β-sheet motifs (or six Kelch repeats).

Kelch is a 50-residue motif, named after the Drosophila mutant in which it was first identified
[1]
. This sequence motif represents one β-sheet blade, and several of these repeats can associate to form a β-propeller. For instance, the motif appears 6 times in Drosophila egg-chamber regulatory protein (also known as ring canal kelch protein), creating a 6-bladed β-propeller. The motif is also found in mouse protein MIPP
[1]
and in a number of poxviruses. In addition, kelch repeats have been recognised in alpha-and beta-scruin
[2, 3]
, and in galactose oxidase from the fungus Dactylium dendroides
[4, 5]
. The structure of galactose oxidase reveals that the repeated sequence corresponds to a 4-stranded antiparallel β-sheet motif that forms the repeat unit in a super-barrel structural fold
[6]
.

The known functions of kelch-containing proteins are diverse: scruin is an actin cross-linking protein; galactose oxidase catalyses the oxidation of the hydroxyl group at the C6 position in D-galactose; and kelch may have a cytoskeletal function, as it is localised to the actin-rich ring canals that connect the 15 nurse cells to the developing oocyte in Drosophila
[2]
. Nevertheless, based on the location of the kelch pattern in the catalytic unit in galactose oxidase, functionally important residues have been predicted in glyoxal oxidase
[4]
.

References

1.kelch encodes a component of intercellular bridges in Drosophila egg chambers. Xue F, Cooley L. Cell 72, 681-93, (1993). View articlePMID: 8453663

2.beta-Scruin, a homologue of the actin crosslinking protein scruin, is localized to the acrosomal vesicle of Limulus sperm. Way M, Sanders M, Chafel M, Tu YH, Knight A, Matsudaira P. J. Cell. Sci. 108 ( Pt 10), 3155-62, (1995). PMID: 7593276

3.Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm. Way M, Sanders M, Garcia C, Sakai J, Matsudaira P. J. Cell Biol. 128, 51-60, (1995). View articlePMID: 7822422

4.Drosophila kelch motif is derived from a common enzyme fold. Bork P, Doolittle RF. J. Mol. Biol. 236, 1277-82, (1994). View articlePMID: 8126718

5.Novel thioether bond revealed by a 1.7 A crystal structure of galactose oxidase. Ito N, Phillips SE, Stevens C, Ogel ZB, McPherson MJ, Keen JN, Yadav KD, Knowles PF. Nature 350, 87-90, (1991). View articlePMID: 2002850

6.Crystal structure of a free radical enzyme, galactose oxidase. Ito N, Phillips SE, Yadav KD, Knowles PF. J. Mol. Biol. 238, 794-814, (1994). View articlePMID: 8182749

GO terms

biological process

  • None

cellular component

  • None

Cross References

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