1sbz
From Proteopedia
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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 with FMN as ligand. 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 Wed Nov 21 02:15:49 2007
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. | FMN | Bsgi | Fmn binding | Montreal-kingston bacterial structural genomics initiative | Pad1 | Structural genomics | Ubix