Structural evidence for dimerization-regulated activation of an integral membrane phospholipase

Dimerization is a biological regulatory mechanism employed by both soluble and membrane proteins. However, there are few structural data on the factors that govern dimerization of membrane proteins. Outer membrane phospholipase A (OMPLA) is an integral membrane enzyme which participates in secretion...

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Veröffentlicht in:	Nature (London) 1999-10, Vol.401 (6754), p.717-721
Hauptverfasser:	SNIJDER, H. J, UBARRETXENA-BELANDIA, I, BLAAUW, M, KALK, K. H, VERHELJ, H. M, EGMOND, M. R, DEKKER, N, DIJKSTRA, B. W
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Bacterial Outer Membrane Proteins - chemistry Bacterial Outer Membrane Proteins - metabolism Binding Sites Biological and medical sciences Crystallography, X-Ray Dimerization Enzyme Activation Enzymes and enzyme inhibitors Escherichia coli Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Hydrolases Models, Molecular Phospholipases A - chemistry Phospholipases A - metabolism
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