1hzd

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1hzd, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF HUMAN AUH PROTEIN, AN RNA-BINDING HOMOLOGUE OF ENOYL-COA HYDRATASE

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

BACKGROUND: The AU binding homolog of enoyl-CoA hydratase (AUH) is a, bifunctional protein that has two distinct activities: AUH binds to RNA, and weakly catalyzes the hydration of 2-trans-enoyl-coenzyme A, (enoyl-CoA). AUH has no sequence similarity with other known RNA binding, proteins, but it has considerable sequence similarity with enoyl-CoA, hydratase. A segment of AUH, named the R peptide, binds to RNA. However, the mechanism of the RNA binding activity of AUH remains to be elucidated., RESULTS: We determined the crystal structure of human AUH at 2.2 A, resolution. AUH adopts the typical fold of the enoyl-CoA, hydratase/isomerase superfamily and forms a hexamer as a dimer of trimers., Interestingly, the surface of the AUH hexamer is positively charged, in, striking contrast to the negatively charged surfaces of the other members, of the superfamily. Furthermore, wide clefts are uniquely formed between, the two trimers of AUH and are highly positively charged with the Lys, residues in alpha helix H1, which is located on the edge of the cleft and, contains the majority of the R peptide. A mutational analysis showed that, the lysine residues in alpha helix H1 are essential to the RNA binding, activity of AUH. CONCLUSIONS: Alpha helix H1 exposes a row of Lys residues, on the solvent-accessible surface. These characteristic Lys residues are, named the "lysine comb." The distances between these Lys residues are, similar to those between the RNA phosphate groups, suggesting that the, lysine comb may continuously bind to a single-stranded RNA. The clefts, between the trimers may provide spaces sufficient to accommodate the RNA, bases.

Disease

Known disease associated with this structure: 3-methylglutaconic aciduria, type I OMIM:[600529]

About this Structure

1HZD is a Single protein structure of sequence from Homo sapiens. Active as Enoyl-CoA hydratase, with EC number 4.2.1.17 Full crystallographic information is available from OCA.

Reference

Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase., Kurimoto K, Fukai S, Nureki O, Muto Y, Yokoyama S, Structure. 2001 Dec;9(12):1253-63. PMID:11738050

Page seeded by OCA on Mon Nov 12 17:24:30 2007