2grv
From Proteopedia
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Crystal Structure of LpqW
Overview
The waxy cell wall is crucial to the survival of mycobacteria within the, infected host. The cell wall is a complex structure rich in unusual, molecules that includes two related lipoglycans, the phosphatidylinositol, mannosides (PIMs) and lipoarabinomannans (LAMs). Many proteins implicated, in the PIM/LAM biosynthetic pathway, while attractive therapeutic targets, are poorly defined. The 2.4A resolution crystal structure of an essential, lipoprotein, LpqW, implicated in LAM biosynthesis is reported here. LpqW, adopts a scaffold reminiscent of the distantly related, promiscuous, substrate-binding proteins of the ATP-binding cassette import system., Nevertheless, the unique closed conformation of LpqW suggests that, mycobacteria and other closely related pathogens have hijacked this, scaffold for use in key processes of cell wall biosynthesis. In silico, docking provided a plausible model in which the candidate PIM ligand binds, within a marked electronegative region located on the surface of LpqW. We, suggest that LpqW represents an archetypal lipoprotein that channels, intermediates from a pathway for mature PIM production into a pathway for, LAM biosynthesis, thus controlling the relative abundance of these two, important components of the cell wall.
About this Structure
2GRV is a Single protein structure of sequence from Mycobacterium smegmatis. Full crystallographic information is available from OCA.
Reference
Hijacking of a substrate-binding protein scaffold for use in mycobacterial cell wall biosynthesis., Marland Z, Beddoe T, Zaker-Tabrizi L, Lucet IS, Brammananth R, Whisstock JC, Wilce MC, Coppel RL, Crellin PK, Rossjohn J, J Mol Biol. 2006 Jun 16;359(4):983-97. Epub 2006 Apr 25. PMID:16698034
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