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2g23

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(New page: 200px<br /><applet load="2g23" size="450" color="white" frame="true" align="right" spinBox="true" caption="2g23, resolution 2.30&Aring;" /> '''The crystal structur...)
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[[Image:2g23.gif|left|200px]]<br /><applet load="2g23" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2g23.gif|left|200px]]<br /><applet load="2g23" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2g23, resolution 2.30&Aring;" />
caption="2g23, resolution 2.30&Aring;" />
'''The crystal structure of hexameric phenoxazinone synthase'''<br />
'''The crystal structure of hexameric phenoxazinone synthase'''<br />
==Overview==
==Overview==
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The multicopper oxidase phenoxazinone synthase (PHS) catalyzes the, penultimate step in the biosynthesis of the antibiotic actinomycin D by, Streptomyces antibioticus. PHS exists in two oligomeric forms: a dimeric, form and a hexameric form, with older actinomycin-producing cultures, containing predominately the hexameric form. The structure of hexameric, PHS has been determined using X-ray diffraction to a resolution limit of, 2.30 A and is found to contain several unexpected and distinctive, features. The structure forms a hexameric ring that is centered on a, pseudo 6-fold axis and has an outer diameter of 185 A with a large central, cavity that has a diameter of 50 A. This hexameric structure is stabilized, by a long loop connecting two domains; bound to this long loop is a fifth, copper atom that is present as a type 2 copper. This copper atom is not, present in any other multicopper oxidase, and its presence appears to, stabilize the hexameric structure.
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The multicopper oxidase phenoxazinone synthase (PHS) catalyzes the penultimate step in the biosynthesis of the antibiotic actinomycin D by Streptomyces antibioticus. PHS exists in two oligomeric forms: a dimeric form and a hexameric form, with older actinomycin-producing cultures containing predominately the hexameric form. The structure of hexameric PHS has been determined using X-ray diffraction to a resolution limit of 2.30 A and is found to contain several unexpected and distinctive features. The structure forms a hexameric ring that is centered on a pseudo 6-fold axis and has an outer diameter of 185 A with a large central cavity that has a diameter of 50 A. This hexameric structure is stabilized by a long loop connecting two domains; bound to this long loop is a fifth copper atom that is present as a type 2 copper. This copper atom is not present in any other multicopper oxidase, and its presence appears to stabilize the hexameric structure.
==About this Structure==
==About this Structure==
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2G23 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_antibioticus Streptomyces antibioticus] with CU, C2O and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2G23 OCA].
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2G23 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_antibioticus Streptomyces antibioticus] with <scene name='pdbligand=CU:'>CU</scene>, <scene name='pdbligand=C2O:'>C2O</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G23 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Streptomyces antibioticus]]
[[Category: Streptomyces antibioticus]]
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[[Category: Allen, J.P.]]
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[[Category: Allen, J P.]]
[[Category: Camara-Artigas, A.]]
[[Category: Camara-Artigas, A.]]
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[[Category: Francisco, W.A.]]
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[[Category: Francisco, W A.]]
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[[Category: Smith, A.W.]]
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[[Category: Smith, A W.]]
[[Category: Wang, M.]]
[[Category: Wang, M.]]
[[Category: C2O]]
[[Category: C2O]]
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[[Category: multicopper oxidase]]
[[Category: multicopper oxidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:54:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:27:26 2008''

Revision as of 15:27, 21 February 2008


2g23, resolution 2.30Å

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The crystal structure of hexameric phenoxazinone synthase

Overview

The multicopper oxidase phenoxazinone synthase (PHS) catalyzes the penultimate step in the biosynthesis of the antibiotic actinomycin D by Streptomyces antibioticus. PHS exists in two oligomeric forms: a dimeric form and a hexameric form, with older actinomycin-producing cultures containing predominately the hexameric form. The structure of hexameric PHS has been determined using X-ray diffraction to a resolution limit of 2.30 A and is found to contain several unexpected and distinctive features. The structure forms a hexameric ring that is centered on a pseudo 6-fold axis and has an outer diameter of 185 A with a large central cavity that has a diameter of 50 A. This hexameric structure is stabilized by a long loop connecting two domains; bound to this long loop is a fifth copper atom that is present as a type 2 copper. This copper atom is not present in any other multicopper oxidase, and its presence appears to stabilize the hexameric structure.

About this Structure

2G23 is a Single protein structure of sequence from Streptomyces antibioticus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of phenoxazinone synthase from Streptomyces antibioticus reveals a new type 2 copper center., Smith AW, Camara-Artigas A, Wang M, Allen JP, Francisco WA, Biochemistry. 2006 Apr 11;45(14):4378-87. PMID:16584173

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