Structural highlights
Function
[YEK0_YEAST] Catalyzes the aldol cleavage of 4-hydroxy-4-methyl-2-oxoglutarate (HMG) into 2 molecules of pyruvate. Also contains a secondary oxaloacetate (OAA) decarboxylase activity due to the common pyruvate enolate transition state formed following C-C bond cleavage in the retro-aldol and decarboxylation reactions.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
We present here the structure of Yer010c protein of unknown function, solved by Multiple Anomalous Diffraction and revealing a common fold and oligomerization state with proteins of the regulator of ribonuclease activity A (RraA) family. In Escherichia coli, RraA has been shown to regulate the activity of ribonuclease E by direct interaction. The absence of ribonuclease E in yeast suggests a different function for this family member in this organism. Yer010cp has a few supplementary secondary structure elements and a deep pseudo-knot at the heart of the protein core. A tunnel at the interface between two monomers, lined with conserved charged residues, has unassigned residual electron density and may constitute an active site for a yet unknown activity.
Crystal structure of yeast YER010Cp, a knotable member of the RraA protein family.,Leulliot N, Quevillon-Cheruel S, Graille M, Schiltz M, Blondeau K, Janin J, Van Tilbeurgh H Protein Sci. 2005 Oct;14(10):2751-8. PMID:16195557[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leulliot N, Quevillon-Cheruel S, Graille M, Schiltz M, Blondeau K, Janin J, Van Tilbeurgh H. Crystal structure of yeast YER010Cp, a knotable member of the RraA protein family. Protein Sci. 2005 Oct;14(10):2751-8. PMID:16195557 doi:14/10/2751
