Literature summary for 3.4.24.B16 extracted from

Spencer, J.; Murphy, L.M.; Conners, R.; Sessions, R.B.; Gamblin, S.J.
Crystal structure of the LasA virulence factor from Pseudomonas aeruginosa: substrate specificity and mechanism of M23 metallopeptidases (2010), J. Mol. Biol., 396, 908-923.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of active LasA as a complex with tartrate and in the uncomplexed form, to 1.28 A resolution. The overall fold resembles that of the other M23 family members, the LasA active site is less constricted and utilizes a different set of metal ligands. The active site of uncomplexed LasA contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules. Manual docking study of the pentapeptide Gly-Gly-Phe-Gly-Gly in the active site so that the carbonyl oxygen of the scissile peptide occupies the approximate position of Tyr151-bound tartrate oxygen O1 and the P2 and P1 glycines follow the path of the tartrate carbon skeleton	Pseudomonas aeruginosa

Crystallization (Comment)

Organism

crystal structures of active LasA as a complex with tartrate and in the uncomplexed form, to 1.28 A resolution. The overall fold resembles that of the other M23 family members, the LasA active site is less constricted and utilizes a different set of metal ligands. The active site of uncomplexed LasA contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules. Manual docking study of the pentapeptide Gly-Gly-Phe-Gly-Gly in the active site so that the carbonyl oxygen of the scissile peptide occupies the approximate position of Tyr151-bound tartrate oxygen O1 and the P2 and P1 glycines follow the path of the tartrate carbon skeleton

Pseudomonas aeruginosa

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zinc	the active site of uncomplexed LasA contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, crystallization data	Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
19963	-	x * 19963, electrospray mass spectrometry, mature protein	Pseudomonas aeruginosa

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas aeruginosa	P14789	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	cleavage of proLasA precursor at position 237 of full-length gene product	Pseudomonas aeruginosa

Purification (Commentary)

Purification (Comment)	Organism
-	Pseudomonas aeruginosa

Reaction

Reaction	Comment	Organism	Reaction ID
proteolytic degradation of proteins	substrate carbonyl oxygen displaces Zn2+-bound water molecule 2, thereby enabling direct interaction with Zn2+ to polarize the peptide carbonyl bond, rendering it susceptible to nucleophilic attack by the second Zn2+-bound water molecule, water molecule1. Water molecule 1 is oriented by interactions with the Nepsilon atoms of both His120 and His81, while that with Zn2+ is weakened. Either of these residues is capable of abstracting a proton from water molecule 1, enabling its addition, as hydroxide, to the substrate carbonyl carbon to generate an oxyanion that is stabilized by bidentate co-ordination of Zn2+ and by interaction with the unprotonated His residue. Proton transfer from the histidine general base to the departing amide nitrogen facilitates cleavage of the peptide bond to generate a product complex	Pseudomonas aeruginosa	a

Subunits

Subunits	Comment	Organism
?	x * 19963, electrospray mass spectrometry, mature protein	Pseudomonas aeruginosa