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| - | [[Image:1mvl.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1mvl| PDB=1mvl | SCENE= }} | | {{STRUCTURE_1mvl| PDB=1mvl | SCENE= }} |
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| - | '''PPC decarboxylase mutant C175S'''
| + | ===PPC decarboxylase mutant C175S=== |
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| - | ==Overview==
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| - | The Arabidopsis thaliana protein AtHAL3a decarboxylates 4'-phosphopantothenoylcysteine to 4'-phosphopantetheine, a step in coenzyme A biosynthesis. Surprisingly, this decarboxylation reaction is carried out as an FMN-dependent redox reaction. In the first half-reaction, the side-chain of the cysteine residue of 4'-phosphopantothenoylcysteine is oxidised and the thioaldehyde intermediate decarboxylates spontaneously to the 4'-phosphopantothenoyl-aminoethenethiol intermediate. In the second half-reaction this compound is reduced to 4'-phosphopantetheine and the FMNH(2) cofactor is re-oxidised. The active site mutant C175S is unable to perform this reductive half-reaction. Here, we present the crystal structure of the AtHAL3a mutant C175S in complex with the reaction intermediate pantothenoyl-aminoethenethiol and FMNH(2). The geometry of binding suggests that reduction of the C(alpha)=C(beta) double bond of the intermediate can be performed by direct hydride-transfer from N5 of FMNH(2) to C(beta) of the aminoethenethiol-moiety supported by a protonation of C(alpha) by Cys175. The binding mode of the substrate is very similar to that previously observed for a pentapeptide to the homologous enzyme EpiD that introduces the aminoethenethiol-moiety as final reaction product at the C terminus of peptidyl-cysteine residues. This finding further supports our view that these homologous enzymes form a protein family of homo-oligomeric flavin-containing cysteine decarboxylases, which we have termed HFCD family. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12614618}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12614618 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12614618}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Flavoprotein]] | | [[Category: Flavoprotein]] |
| | [[Category: Ppc decarboxylase]] | | [[Category: Ppc decarboxylase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:46:25 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:26:05 2008'' |
Revision as of 17:26, 28 July 2008
Template:STRUCTURE 1mvl
PPC decarboxylase mutant C175S
Template:ABSTRACT PUBMED 12614618
About this Structure
1MVL is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
Crystal structure of the plant PPC decarboxylase AtHAL3a complexed with an ene-thiol reaction intermediate., Steinbacher S, Hernandez-Acosta P, Bieseler B, Blaesse M, Huber R, Culianez-Macia FA, Kupke T, J Mol Biol. 2003 Mar 14;327(1):193-202. PMID:12614618
Page seeded by OCA on Mon Jul 28 20:26:05 2008
