1y9i

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Revision as of 01:38, 25 November 2007

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spinqualitylabelsall models 1y9i, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of low temperature requirement C protein from Listeria monocytogenes

Overview

Phosphatidylglycerophosphatase (PGPase), an enzyme involved in lipid, metabolism, catalyzes formation of phosphatidylglycerol from, phosphatidylglycerophosphate. Phosphatidylglycerol is a multifunctional, phospholipid, found in the biological membranes of many organisms. Here, we report the crystal structure of Listeria monocytogenes PGPase at 1.8 A, resolution. PGPase, an all-helical molecule, forms a homotetramer. Each, protomer contains an independent active site with two metal ions, Ca(2+), and Mg(2+), forming a hetero-binuclear center located in a hydrophilic, cavity near the surface of the molecule. The binuclear center, conserved, ligands, metal-bound water molecules, and an Asp-His dyad form the active, site. The catalytic mechanism of this enzyme is likely to proceed via, binuclear metal activated nucleophilic water. The binuclear metal-binding, active-site environment of this structure should provide insights into, substrate binding and metal-dependent catalysis. A long channel with, inter-linked linear water chains, termed "proton wires," is observed at, the tetramer interface. Comparison of similar water chain structures in, photosynthetic reaction centers (RCs), Cytochrome f, gramicidin, and, bacteriorhodopsin, suggests that PGPase may conduct protons via proton, wires.

About this Structure

1Y9I is a Single protein structure of sequence from Listeria monocytogenes with CA, MG and GOL as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of phosphatidylglycerophosphatase (PGPase), a putative membrane-bound lipid phosphatase, reveals a novel binuclear metal binding site and two "proton wires"., Kumaran D, Bonanno JB, Burley SK, Swaminathan S, Proteins. 2006 Sep 1;64(4):851-62. PMID:16838328

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