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1lq9

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(New page: 200px<br /><applet load="1lq9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lq9, resolution 1.30&Aring;" /> '''Crystal Structure of...)
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[[Image:1lq9.jpg|left|200px]]<br /><applet load="1lq9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lq9, resolution 1.30&Aring;" />
caption="1lq9, resolution 1.30&Aring;" />
'''Crystal Structure of a Monooxygenase from the Gene ActVA-Orf6 of Streptomyces coelicolor Strain A3(2)'''<br />
'''Crystal Structure of a Monooxygenase from the Gene ActVA-Orf6 of Streptomyces coelicolor Strain A3(2)'''<br />
==Overview==
==Overview==
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ActVA-Orf6 monooxygenase from Streptomyces coelicolor that catalyses the, oxidation of an aromatic intermediate of the actinorhodin biosynthetic, pathway is a member of a class of small monooxygenases that carry out, oxygenation without the assistance of any of the prosthetic groups, metal, ions or cofactors normally associated with activation of molecular oxygen., The overall structure is a ferredoxin-like fold with a novel dimeric, assembly, indicating that the widely represented ferredoxin fold may, sustain yet another functionality. The resolution (1.3 A) of the enzyme, structure and its complex with substrate and product analogues allows us, to visualize the mechanism of binding and activation of the substrate for, attack by molecular oxygen, and utilization of two gates for the reaction, components including a proton gate and an O(2)/H(2)O gate with a putative, protein channel. This is the first crystal structure of an enzyme involved, in the tailoring of a type II aromatic polyketide and illustrates some of, the enzyme-substrate recognition features that may apply to a range of, other enzymes involved in modifying a polyketide core structure.
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ActVA-Orf6 monooxygenase from Streptomyces coelicolor that catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway is a member of a class of small monooxygenases that carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The overall structure is a ferredoxin-like fold with a novel dimeric assembly, indicating that the widely represented ferredoxin fold may sustain yet another functionality. The resolution (1.3 A) of the enzyme structure and its complex with substrate and product analogues allows us to visualize the mechanism of binding and activation of the substrate for attack by molecular oxygen, and utilization of two gates for the reaction components including a proton gate and an O(2)/H(2)O gate with a putative protein channel. This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme-substrate recognition features that may apply to a range of other enzymes involved in modifying a polyketide core structure.
==About this Structure==
==About this Structure==
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1LQ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with PG4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LQ9 OCA].
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1LQ9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor] with <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQ9 OCA].
==Reference==
==Reference==
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[[Category: Streptomyces coelicolor]]
[[Category: Streptomyces coelicolor]]
[[Category: Federici, L.]]
[[Category: Federici, L.]]
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[[Category: Kendrew, S.G.]]
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[[Category: Kendrew, S G.]]
[[Category: Malatesta, F.]]
[[Category: Malatesta, F.]]
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[[Category: Marsh, N.G.]]
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[[Category: Marsh, N G.]]
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[[Category: Miele, A.E.]]
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[[Category: Miele, A E.]]
[[Category: Savino, C.]]
[[Category: Savino, C.]]
[[Category: Schimperna, G.]]
[[Category: Schimperna, G.]]
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[[Category: streptomyces coelicolor]]
[[Category: streptomyces coelicolor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:15:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:47:27 2008''

Revision as of 11:47, 21 February 2008


1lq9, resolution 1.30Å

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Crystal Structure of a Monooxygenase from the Gene ActVA-Orf6 of Streptomyces coelicolor Strain A3(2)

Overview

ActVA-Orf6 monooxygenase from Streptomyces coelicolor that catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway is a member of a class of small monooxygenases that carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The overall structure is a ferredoxin-like fold with a novel dimeric assembly, indicating that the widely represented ferredoxin fold may sustain yet another functionality. The resolution (1.3 A) of the enzyme structure and its complex with substrate and product analogues allows us to visualize the mechanism of binding and activation of the substrate for attack by molecular oxygen, and utilization of two gates for the reaction components including a proton gate and an O(2)/H(2)O gate with a putative protein channel. This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme-substrate recognition features that may apply to a range of other enzymes involved in modifying a polyketide core structure.

About this Structure

1LQ9 is a Single protein structure of sequence from Streptomyces coelicolor with as ligand. Full crystallographic information is available from OCA.

Reference

The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis., Sciara G, Kendrew SG, Miele AE, Marsh NG, Federici L, Malatesta F, Schimperna G, Savino C, Vallone B, EMBO J. 2003 Jan 15;22(2):205-15. PMID:12514126

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