1k3i

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Crystal Structure of the Precursor of Galactose Oxidase

Structural highlights

1k3i is a 1 chain structure with sequence from Fusarium sp.. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Ligands:ACT, CA, CSO, GLC
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GAOA_GIBZA Catalyzes the sterospecific oxidation of primary alcohols to the corresponding aldehydes. The biologically relevant substrate of the enzyme is not known as the enzyme exhibits broad substrate specificity from small alcohols through sugars to oligo- and polysaccharides.[1] [2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Galactose oxidase (EC ) is a monomeric enzyme that contains a single copper ion and catalyses the stereospecific oxidation of primary alcohols to their corresponding aldehydes. The protein contains an unusual covalent thioether bond between a tyrosine, which acts as a radical center during the two-electron reaction, and a cysteine. The enzyme is produced in a precursor form lacking the thioether bond and also possessing an additional 17-aa pro-sequence at the N terminus. Previous work has shown that the aerobic addition of Cu(2+) to the precursor is sufficient to generate fully processed mature enzyme. The structure of the precursor protein has been determined to 1.4 A, revealing the location of the pro-sequence and identifying structural differences between the precursor and the mature protein. Structural alignment of the precursor and mature forms of galactose oxidase shows that five regions of main chain and some key residues of the active site differ significantly between the two forms. The precursor structure provides a starting point for modeling the chemistry of thioether bond formation and pro-sequence cleavage.

Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme.,Firbank SJ, Rogers MS, Wilmot CM, Dooley DM, Halcrow MA, Knowles PF, McPherson MJ, Phillips SE Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):12932-7. PMID:11698678[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
11 reviews cite this structure
Structural and functional diversity of lectin repertoires in invertebrates, protochordates and ectothermic vertebrates.
Vasta et al. (2004)
10 more
39 other articles
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See Also

References

  1. ↑ COOPER JA, SMITH W, BACILA M, MEDINA H. Galactose oxidase from Polyporus circinatus, Fr. J Biol Chem. 1959 Mar;234(3):445-8 PMID:13641238
  2. ↑ Kosman DJ, Ettinger MJ, Weiner RE, Massaro EJ. The molecular properties of the copper enzyme galactose oxidase. Arch Biochem Biophys. 1974 Dec;165(2):456-67. PMID:4441089 doi:10.1016/0003-9861(74)90271-9
  3. ↑ Firbank SJ, Rogers MS, Wilmot CM, Dooley DM, Halcrow MA, Knowles PF, McPherson MJ, Phillips SE. Crystal structure of the precursor of galactose oxidase: an unusual self-processing enzyme. Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):12932-7. PMID:11698678 doi:http://dx.doi.org/10.1073/pnas.231463798

Contents


PDB ID 1k3i

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