1sbz

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(New page: 200px<br /><applet load="1sbz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sbz, resolution 2.00&Aring;" /> '''Crystal Structure of...)
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[[Image:1sbz.gif|left|200px]]<br /><applet load="1sbz" size="350" color="white" frame="true" align="right" spinBox="true"
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'''Crystal Structure of dodecameric FMN-dependent Ubix-like Decarboxylase from Escherichia coli O157:H7'''<br />
'''Crystal Structure of dodecameric FMN-dependent Ubix-like Decarboxylase from Escherichia coli O157:H7'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1SBZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SBZ OCA].
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1SBZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SBZ OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: BSGI, Montreal-Kingston.Bacterial.Structural.Genomics.Initiative.]]
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[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
[[Category: Cygler, M.]]
[[Category: Cygler, M.]]
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[[Category: Hung, L.W.]]
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[[Category: Hung, L W.]]
[[Category: Iannuzzi, P.]]
[[Category: Iannuzzi, P.]]
[[Category: Li, Y.]]
[[Category: Li, Y.]]
[[Category: Matte, A.]]
[[Category: Matte, A.]]
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[[Category: Rangarajan, E.S.]]
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[[Category: Rangarajan, E S.]]
[[Category: Tocilj, A.]]
[[Category: Tocilj, A.]]
[[Category: FMN]]
[[Category: FMN]]
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[[Category: ubix]]
[[Category: ubix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:59 2008''

Revision as of 13:00, 21 February 2008


1sbz, resolution 2.00Å

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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 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

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