Literature summary for 3.4.23.48 extracted from

Eren, E.; Murphy, M.; Goguen, J.; van den Berg, B.
An active site water network in the plasminogen activator pla from Yersinia pestis (2010), Structure, 18, 809-818.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
wild-type, to 1.9 A, and inactive mutant D86A, to 2.5 A resolution, respectively. The structure shows a water molecule located between active site residues D84 and H208, and a number of other water molecules. The R211 side-chain in loop L4 is close to the nucleophilic water and possibly involved in the stabilization of the oxyanion intermediate. Subtle conformational changes of H208 result from the binding of lipopolysaccharide to the outside of the barrel, explaining the unusual dependence of omptins on lipopolysaccharide for activity	Yersinia pestis

Crystallization (Comment)

Organism

wild-type, to 1.9 A, and inactive mutant D86A, to 2.5 A resolution, respectively. The structure shows a water molecule located between active site residues D84 and H208, and a number of other water molecules. The R211 side-chain in loop L4 is close to the nucleophilic water and possibly involved in the stabilization of the oxyanion intermediate. Subtle conformational changes of H208 result from the binding of lipopolysaccharide to the outside of the barrel, explaining the unusual dependence of omptins on lipopolysaccharide for activity

Yersinia pestis

Protein Variants

Protein Variants	Comment	Organism
D86A	inactive, crystallization data	Yersinia pestis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining

Organism

Organism	UniProt	Comment	Textmining
Yersinia pestis	P17811	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
Converts human Glu-plasminogen to plasmin by cleaving the Arg560-/-Val peptide bond that is also hydrolysed by the mammalian u-plasminogen activator and t-plasminogen activator. Also cleaves arginyl bonds in other proteins	distribution of residues within the active site cleft strongly suggests that the arginine side chain of the substrate will bind in a deep, negatively charged pocket formed by Pla residues E29, D204, D206, and E217. The two valine residues C-terminal to the scissile bond will likely bind in the shallow, hydrophobic pocket located on the other side of the plane formed by the active site residues D84, H208, and the nucleophilic water molecule	Yersinia pestis	a