1tuw
From Proteopedia
(New page: 200px<br /><applet load="1tuw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tuw, resolution 1.9Å" /> '''Structural and Functi...) |
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| - | [[Image:1tuw.jpg|left|200px]]<br /><applet load="1tuw" size=" | + | [[Image:1tuw.jpg|left|200px]]<br /><applet load="1tuw" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1tuw, resolution 1.9Å" /> | caption="1tuw, resolution 1.9Å" /> | ||
'''Structural and Functional Analysis of Tetracenomycin F2 Cyclase from Streptomyces glaucescens: A Type-II Polyketide Cyclase'''<br /> | '''Structural and Functional Analysis of Tetracenomycin F2 Cyclase from Streptomyces glaucescens: A Type-II Polyketide Cyclase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tetracenomycin F2 cyclase (tcmI gene product), catalyzes an aromatic | + | Tetracenomycin F2 cyclase (tcmI gene product), catalyzes an aromatic rearrangement in the biosynthetic pathway for tetracenomycin C in Streptomyces glaucescens. The x-ray structure of this small enzyme has been determined to 1.9-A resolution together with an analysis of site-directed mutants of potential catalytic residues. The protein exhibits a dimeric betaalphabeta ferredoxin-like fold that utilizes strand swapping between subunits in its assembly. The fold is dominated by four strands of antiparallel sheet and a layer of alpha-helices, which creates a cavity that is proposed to be the active site. This type of secondary structural arrangement has been previously observed in polyketide monooxygenases and suggests an evolutionary relationship between enzymes that catalyze adjacent steps in these biosynthetic pathways. Mutational analysis of all of the obvious catalytic bases within the active site suggests that the enzyme functions to steer the chemical outcome of the cyclization rather than providing a specific catalytic group. Together, the structure and functional analysis provide insight into the structural framework necessary to perform the complex rearrangements catalyzed by this class of polyketide cyclases. |
==About this Structure== | ==About this Structure== | ||
| - | 1TUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_glaucescens Streptomyces glaucescens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TUW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_glaucescens Streptomyces glaucescens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces glaucescens]] | [[Category: Streptomyces glaucescens]] | ||
| - | [[Category: Hutchinson, C | + | [[Category: Hutchinson, C R.]] |
[[Category: Katayama, K.]] | [[Category: Katayama, K.]] | ||
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: Thompson, T | + | [[Category: Thompson, T B.]] |
[[Category: Watanabe, K.]] | [[Category: Watanabe, K.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: dimeric ??? ferredoxin-like fold tetracenomycin c biosynthesis]] | [[Category: dimeric ??? ferredoxin-like fold tetracenomycin c biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:38 2008'' |
Revision as of 13:17, 21 February 2008
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Structural and Functional Analysis of Tetracenomycin F2 Cyclase from Streptomyces glaucescens: A Type-II Polyketide Cyclase
Overview
Tetracenomycin F2 cyclase (tcmI gene product), catalyzes an aromatic rearrangement in the biosynthetic pathway for tetracenomycin C in Streptomyces glaucescens. The x-ray structure of this small enzyme has been determined to 1.9-A resolution together with an analysis of site-directed mutants of potential catalytic residues. The protein exhibits a dimeric betaalphabeta ferredoxin-like fold that utilizes strand swapping between subunits in its assembly. The fold is dominated by four strands of antiparallel sheet and a layer of alpha-helices, which creates a cavity that is proposed to be the active site. This type of secondary structural arrangement has been previously observed in polyketide monooxygenases and suggests an evolutionary relationship between enzymes that catalyze adjacent steps in these biosynthetic pathways. Mutational analysis of all of the obvious catalytic bases within the active site suggests that the enzyme functions to steer the chemical outcome of the cyclization rather than providing a specific catalytic group. Together, the structure and functional analysis provide insight into the structural framework necessary to perform the complex rearrangements catalyzed by this class of polyketide cyclases.
About this Structure
1TUW is a Single protein structure of sequence from Streptomyces glaucescens with as ligand. Full crystallographic information is available from OCA.
Reference
Structural and functional analysis of tetracenomycin F2 cyclase from Streptomyces glaucescens. A type II polyketide cyclase., Thompson TB, Katayama K, Watanabe K, Hutchinson CR, Rayment I, J Biol Chem. 2004 Sep 3;279(36):37956-63. Epub 2004 Jun 30. PMID:15231835
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