1k3i

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(New page: 200px<br /><applet load="1k3i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k3i, resolution 1.40&Aring;" /> '''Crystal Structure of...)
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caption="1k3i, resolution 1.40&Aring;" />
caption="1k3i, resolution 1.40&Aring;" />
'''Crystal Structure of the Precursor of Galactose Oxidase'''<br />
'''Crystal Structure of the Precursor of Galactose Oxidase'''<br />
==Overview==
==Overview==
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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.
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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.
==About this Structure==
==About this Structure==
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1K3I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sp. Fusarium sp.] with GLC, CA and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Galactose_oxidase Galactose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.9 1.1.3.9] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K3I OCA].
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1K3I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Fusarium_sp. Fusarium sp.] with <scene name='pdbligand=GLC:'>GLC</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Galactose_oxidase Galactose oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.3.9 1.1.3.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K3I OCA].
==Reference==
==Reference==
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[[Category: Galactose oxidase]]
[[Category: Galactose oxidase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Dooley, D.M.]]
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[[Category: Dooley, D M.]]
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[[Category: Firbank, S.J.]]
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[[Category: Firbank, S J.]]
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[[Category: Halcrow, M.A.]]
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[[Category: Halcrow, M A.]]
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[[Category: Knowles, P.F.]]
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[[Category: Knowles, P F.]]
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[[Category: McPherson, M.J.]]
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[[Category: McPherson, M J.]]
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[[Category: Phillips, S.E.V.]]
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[[Category: Phillips, S E.V.]]
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[[Category: Rogers, M.S.]]
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[[Category: Rogers, M S.]]
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[[Category: Wilmot, C.M.]]
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[[Category: Wilmot, C M.]]
[[Category: ACT]]
[[Category: ACT]]
[[Category: CA]]
[[Category: CA]]
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[[Category: prosequence form]]
[[Category: prosequence form]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:49:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:29:46 2008''

Revision as of 11:29, 21 February 2008


1k3i, resolution 1.40Å

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Crystal Structure of the Precursor of Galactose Oxidase

Overview

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.

About this Structure

1K3I is a Single protein structure of sequence from Fusarium sp. with , and as ligands. Active as Galactose oxidase, with EC number 1.1.3.9 Full crystallographic information is available from OCA.

Reference

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

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