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| | {{STRUCTURE_2pvz| PDB=2pvz | SCENE= }} | | {{STRUCTURE_2pvz| PDB=2pvz | SCENE= }} |
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| - | '''Crystal structure of methylaconitate isomerase PrpF from Shewanella oneidensis'''
| + | ===Crystal structure of methylaconitate isomerase PrpF from Shewanella oneidensis=== |
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| - | ==Overview==
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| - | In bacteria, the dehydration of 2-methylcitrate to yield 2-methylaconitate in the 2-methylcitric acid cycle is catalyzed by a cofactor-less (PrpD) enzyme or by an aconitase-like (AcnD) enzyme. Bacteria that use AcnD also require the function of the PrpF protein, whose function was previously unknown. To gain insights into the function of PrpF, the three-dimensional crystal structure of the PrpF protein from the bacterium Shewanella oneidensis was solved at 2.0 A resolution. The protein fold of PrpF is strikingly similar to those of the non-PLP-dependent diaminopimelate epimerase from Haemophilus influenzae, a putative proline racemase from Brucella melitensis, and to a recently deposited structure of a hypothetical protein from Pseudomonas aeruginosa. Results from in vitro studies show that PrpF isomerizes trans-aconitate to cis-aconitate. It is proposed that PrpF catalysis of the cis-trans isomerization proceeds through a base-catalyzed proton abstraction coupled with a rotation about C2-C3 bond of 2-methylaconitate, and that residue Lys73 is critical for PrpF function. The newly identified function of PrpF as a non-PLP-dependent isomerase, together with the fact that PrpD-containing bacteria do not require PrpF, suggest that the isomer of 2-methylaconitate that serves as a substrate of aconitase must have the same stereochemistry as that synthesized by PrpD. From this, it follows that the 2-methylaconitate isomer generated by AcnD is not a substrate of aconitase, and that PrpF is required to generate the correct isomer. As a consequence, the isomerase activity of PrpF may now be viewed as an integral part of the 2-methylcitric acid cycle.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17567742}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17567742 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17567742}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Propionate catabolism]] | | [[Category: Propionate catabolism]] |
| | [[Category: Unknown function]] | | [[Category: Unknown function]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 13:53:20 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:49:35 2008'' |
Revision as of 11:49, 28 July 2008
Template:STRUCTURE 2pvz
Crystal structure of methylaconitate isomerase PrpF from Shewanella oneidensis
Template:ABSTRACT PUBMED 17567742
About this Structure
2PVZ is a Single protein structure of sequence from Shewanella oneidensis. Full crystallographic information is available from OCA.
Reference
The three-dimensional crystal structure of the PrpF protein of Shewanella oneidensis complexed with trans-aconitate: insights into its biological function., Garvey GS, Rocco CJ, Escalante-Semerena JC, Rayment I, Protein Sci. 2007 Jul;16(7):1274-84. Epub 2007 Jun 13. PMID:17567742
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