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 | 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 Maximum [Da] | Comment | Organism |
---|---|---|---|
19963 | - |
x * 19963, electrospray mass spectrometry, mature protein | Pseudomonas aeruginosa |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | P14789 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | cleavage of proLasA precursor at position 237 of full-length gene product | Pseudomonas aeruginosa |
Purification (Comment) | Organism |
---|---|
- |
Pseudomonas aeruginosa |
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 |
Subunits | Comment | Organism |
---|---|---|
? | x * 19963, electrospray mass spectrometry, mature protein | Pseudomonas aeruginosa |