1g8j

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(New page: 200px<br /><applet load="1g8j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g8j, resolution 2.03&Aring;" /> '''CRYSTAL STRUCTURE AN...)
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'''CRYSTAL STRUCTURE ANALYSIS OF ARSENITE OXIDASE FROM ALCALIGENES FAECALIS'''<br />
'''CRYSTAL STRUCTURE ANALYSIS OF ARSENITE OXIDASE FROM ALCALIGENES FAECALIS'''<br />
==Overview==
==Overview==
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BACKGROUND: Arsenite oxidase from Alcaligenes faecalis NCIB 8687 is a, molybdenum/iron protein involved in the detoxification of arsenic. It is, induced by the presence of AsO(2-) (arsenite) and functions to oxidize, As(III)O(2-), which binds to essential sulfhydryl groups of proteins and, dithiols, to the relatively less toxic As(V)O(4)(3-) (arsenate) prior to, methylation. RESULTS: Using a combination of multiple isomorphous, replacement with anomalous scattering (MIRAS) and multiple-wavelength, anomalous dispersion (MAD) methods, the crystal structure of arsenite, oxidase was determined to 2.03 A in a P2(1) crystal form with two, molecules in the asymmetric unit and to 1.64 A in a P1 crystal form with, four molecules in the asymmetric unit. Arsenite oxidase consists of a, large subunit of 825 residues and a small subunit of approximately 134, residues. The large subunit contains a Mo site, consisting of a Mo atom, bound to two pterin cofactors, and a [3Fe-4S] cluster. The small subunit, contains a Rieske-type [2Fe-2S] site. CONCLUSIONS: The large subunit of, arsenite oxidase is similar to other members of the dimethylsulfoxide, (DMSO) reductase family of molybdenum enzymes, particularly the, dissimilatory periplasmic nitrate reductase from Desulfovibrio, desulfuricans, but is unique in having no covalent bond between the, polypeptide and the Mo atom. The small subunit has no counterpart among, known Mo protein structures but is homologous to the Rieske [2Fe-2S], protein domain of the cytochrome bc(1) and cytochrome b(6)f complexes and, to the Rieske domain of naphthalene 1,2-dioxygenase.
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BACKGROUND: Arsenite oxidase from Alcaligenes faecalis NCIB 8687 is a molybdenum/iron protein involved in the detoxification of arsenic. It is induced by the presence of AsO(2-) (arsenite) and functions to oxidize As(III)O(2-), which binds to essential sulfhydryl groups of proteins and dithiols, to the relatively less toxic As(V)O(4)(3-) (arsenate) prior to methylation. RESULTS: Using a combination of multiple isomorphous replacement with anomalous scattering (MIRAS) and multiple-wavelength anomalous dispersion (MAD) methods, the crystal structure of arsenite oxidase was determined to 2.03 A in a P2(1) crystal form with two molecules in the asymmetric unit and to 1.64 A in a P1 crystal form with four molecules in the asymmetric unit. Arsenite oxidase consists of a large subunit of 825 residues and a small subunit of approximately 134 residues. The large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors, and a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site. CONCLUSIONS: The large subunit of arsenite oxidase is similar to other members of the dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes, particularly the dissimilatory periplasmic nitrate reductase from Desulfovibrio desulfuricans, but is unique in having no covalent bond between the polypeptide and the Mo atom. The small subunit has no counterpart among known Mo protein structures but is homologous to the Rieske [2Fe-2S] protein domain of the cytochrome bc(1) and cytochrome b(6)f complexes and to the Rieske domain of naphthalene 1,2-dioxygenase.
==About this Structure==
==About this Structure==
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1G8J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis] with MGD, O, 4MO, F3S and FES as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G8J OCA].
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1G8J is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis] with <scene name='pdbligand=MGD:'>MGD</scene>, <scene name='pdbligand=O:'>O</scene>, <scene name='pdbligand=4MO:'>4MO</scene>, <scene name='pdbligand=F3S:'>F3S</scene> and <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G8J OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Conrads, T.]]
[[Category: Conrads, T.]]
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[[Category: Ellis, P.J.]]
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[[Category: Ellis, P J.]]
[[Category: Hille, R.]]
[[Category: Hille, R.]]
[[Category: Kuhn, P.]]
[[Category: Kuhn, P.]]
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[[Category: rieske]]
[[Category: rieske]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:47:19 2008''

Revision as of 10:47, 21 February 2008

Image:1g8j.jpg

1g8j, resolution 2.03Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE ANALYSIS OF ARSENITE OXIDASE FROM ALCALIGENES FAECALIS

Overview

BACKGROUND: Arsenite oxidase from Alcaligenes faecalis NCIB 8687 is a molybdenum/iron protein involved in the detoxification of arsenic. It is induced by the presence of AsO(2-) (arsenite) and functions to oxidize As(III)O(2-), which binds to essential sulfhydryl groups of proteins and dithiols, to the relatively less toxic As(V)O(4)(3-) (arsenate) prior to methylation. RESULTS: Using a combination of multiple isomorphous replacement with anomalous scattering (MIRAS) and multiple-wavelength anomalous dispersion (MAD) methods, the crystal structure of arsenite oxidase was determined to 2.03 A in a P2(1) crystal form with two molecules in the asymmetric unit and to 1.64 A in a P1 crystal form with four molecules in the asymmetric unit. Arsenite oxidase consists of a large subunit of 825 residues and a small subunit of approximately 134 residues. The large subunit contains a Mo site, consisting of a Mo atom bound to two pterin cofactors, and a [3Fe-4S] cluster. The small subunit contains a Rieske-type [2Fe-2S] site. CONCLUSIONS: The large subunit of arsenite oxidase is similar to other members of the dimethylsulfoxide (DMSO) reductase family of molybdenum enzymes, particularly the dissimilatory periplasmic nitrate reductase from Desulfovibrio desulfuricans, but is unique in having no covalent bond between the polypeptide and the Mo atom. The small subunit has no counterpart among known Mo protein structures but is homologous to the Rieske [2Fe-2S] protein domain of the cytochrome bc(1) and cytochrome b(6)f complexes and to the Rieske domain of naphthalene 1,2-dioxygenase.

About this Structure

1G8J is a Protein complex structure of sequences from Alcaligenes faecalis with , , , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 A and 2.03 A., Ellis PJ, Conrads T, Hille R, Kuhn P, Structure. 2001 Feb 7;9(2):125-32. PMID:11250197[[Category: [2fe-2s] cluster]] [[Category: [3fe-4s] cluster]]

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