3U0V

Crystal Structure Analysis of human LYPLAL1

Summary for 3U0V

• Entry DOI: 10.2210/pdb3u0v/pdb
• Descriptor: Lysophospholipase-like protein 1 (2 entities in total)
• Functional Keywords: alpha, beta hydrolase fold, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity): Q5VWZ2
• Total number of polymer chains: 1
• Total formula weight: 26521.64

Authors

Burger, M.,Zimmermann, T.J.,Kondoh, Y.,Stege, P.,Watanabe, N.,Osada, H.,Waldmann, H.,Vetter, I.R. (deposition date: 2011-09-29, release date: 2011-11-16, Last modification date: 2023-11-01)

Primary citation

Burger, M.,Zimmermann, T.J.,Kondoh, Y.,Stege, P.,Watanabe, N.,Osada, H.,Waldmann, H.,Vetter, I.R.
Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterases
J.Lipid Res., 53:43-50, 2012

PubMed Abstract: Sequence homology indicates the existence of three human cytosolic acyl protein thioesterases, including APT1 that is known to depalmitoylate H- and N-Ras. One of them is the lysophospholipase-like 1 (LYPLAL1) protein that on the one hand is predicted to be closely related to APT1 but on the other hand might also function as a potential triacylglycerol lipase involved in obesity. However, its role remained unclear. The 1.7 Å crystal structure of LYPLAL1 reveals a fold very similar to APT1, as expected, but features a shape of the active site that precludes binding of long-chain substrates. Biochemical data demonstrate that LYPLAL1 exhibits neither phospholipase nor triacylglycerol lipase activity, but rather accepts short-chain substrates. Furthermore, extensive screening efforts using chemical array technique revealed a first small molecule inhibitor of LYPLAL1.

PubMed: 22052940
DOI: 10.1194/jlr.M019851

Experimental method

X-RAY DIFFRACTION (1.72 Å)