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1sbz
From Proteopedia
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'''Crystal Structure of dodecameric FMN-dependent Ubix-like Decarboxylase from Escherichia coli O157:H7''' | '''Crystal Structure of dodecameric FMN-dependent Ubix-like Decarboxylase from Escherichia coli O157:H7''' | ||
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[[Category: Rangarajan, E S.]] | [[Category: Rangarajan, E S.]] | ||
[[Category: Tocilj, A.]] | [[Category: Tocilj, A.]] | ||
| - | [[Category: | + | [[Category: Bsgi]] |
| - | [[Category: | + | [[Category: Fmn binding]] |
| - | [[Category: | + | [[Category: Montreal-kingston bacterial structural genomics initiative]] |
| - | [[Category: | + | [[Category: Pad1]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: | + | [[Category: Ubix]] |
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Revision as of 05:31, 3 May 2008
Crystal Structure of dodecameric FMN-dependent Ubix-like Decarboxylase from Escherichia coli O157:H7
Overview
The crystal structure of the flavoprotein Pad1 from Escherichia coli O157:H7 complexed with the cofactor FMN has been determined by the multiple anomalous diffraction method and refined at 2.0 A resolution. This protein is a paralog of UbiX (3-octaprenyl-4-hydroxybenzoate carboxylyase, 51% sequence identity) that catalyzes the third step in ubiquinone biosynthesis and to Saccharomyces cerevisiae Pad1 (54% identity), an enzyme that confers resistance to the antimicrobial compounds phenylacrylic acids through decarboxylation of these compounds. Each Pad1 monomer consists of a typical Rossmann fold containing a non-covalently bound molecule of FMN. The fold of Pad1 is similar to MrsD, an enzyme associated with lantibiotic synthesis; EpiD, a peptidyl-cysteine decarboxylase; and AtHAL3a, the enzyme, which decarboxylates 4'-phosphopantothenoylcysteine to 4'-phosphopantetheine during coenzyme A biosynthesis, all with a similar location of the FMN binding site at the interface between two monomers, yet each having little sequence similarity to one another. All of these proteins associate into oligomers, with a trimer forming the common structural unit in each case. In MrsD and EpiD, which belong to the homo-dodecameric flavin-containing cysteine decarboxylase (HFCD) family, these trimers associate further into dodecamers. Pad1 also forms dodecamers, although the association of the trimers is completely different, resulting in exposure of a different side of the trimer unit to the solvent. This exposure affects the location of the substrate binding site and, specifically, its access to the FMN cofactor. Therefore, Pad1 forms a separate family, distinguishable from the HFCD family.
About this Structure
1SBZ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of a dodecameric FMN-dependent UbiX-like decarboxylase (Pad1) from Escherichia coli O157: H7., Rangarajan ES, Li Y, Iannuzzi P, Tocilj A, Hung LW, Matte A, Cygler M, Protein Sci. 2004 Nov;13(11):3006-16. Epub 2004 Sep 30. PMID:15459342 Page seeded by OCA on Sat May 3 08:31:44 2008
Categories: Escherichia coli | Single protein | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Cygler, M. | Hung, L W. | Iannuzzi, P. | Li, Y. | Matte, A. | Rangarajan, E S. | Tocilj, A. | Bsgi | Fmn binding | Montreal-kingston bacterial structural genomics initiative | Pad1 | Structural genomic | Ubix
