1tuw
From Proteopedia
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|PDB= 1tuw |SIZE=350|CAPTION= <scene name='initialview01'>1tuw</scene>, resolution 1.9Å | |PDB= 1tuw |SIZE=350|CAPTION= <scene name='initialview01'>1tuw</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= TCMI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1907 Streptomyces glaucescens]) | |GENE= TCMI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1907 Streptomyces glaucescens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuw OCA], [http://www.ebi.ac.uk/pdbsum/1tuw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tuw RCSB]</span> | ||
}} | }} | ||
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[[Category: Thompson, T B.]] | [[Category: Thompson, T B.]] | ||
[[Category: Watanabe, K.]] | [[Category: Watanabe, K.]] | ||
| - | [[Category: SO4]] | ||
[[Category: dimeric ??? ferredoxin-like fold tetracenomycin c biosynthesis]] | [[Category: dimeric ??? ferredoxin-like fold tetracenomycin c biosynthesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:28 2008'' |
Revision as of 21:01, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | TCMI (Streptomyces glaucescens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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