1GO7

The metzincin's methionine: PrtC M226C-E189K double mutant

Summary for 1GO7

• Entry DOI: 10.2210/pdb1go7/pdb
• Related: 1GO8
• Descriptor: PROTEASE C, CALCIUM ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: hydrolase, protease, metalloprotease
• Biological source: ERWINIA CHRYSANTHEMI
• Cellular location: Secreted: P16317
• Total number of polymer chains: 1
• Total formula weight: 50179.10

Authors

Hege, T. (deposition date: 2001-10-20, release date: 2002-10-17, Last modification date: 2024-05-01)

Primary citation

Hege, T.,Feltzer, R.E.,Gray, R.D.,Baumann, U.
Crystal Structure of a Complex between Pseudomonas Aeruginosa Alkaline Protease and its Cognate Inhibitor: Inhibition by a Zinc-NH2 Coordinative Bond
J.Biol.Chem., 276:35087-, 2001

PubMed Abstract: Serralysins are a family of metalloproteases secreted by Gram-negative bacteria into the medium in the form of inactive zymogens. Usually, all serralysin secretors have on the same operon a gene coding for a periplasmic 10-kDa protein, which is an inhibitor of the secreted protease. The recent characterization of the inhibitor of the alkaline protease from Pseudomonas aeruginosa revealed a surprisingly low dissociation constant of 4 pm, contrary to earlier studies on homologous systems, where inhibition constants in the microm range were reported. To approach a more accurate understanding, the crystal structure of the complex between inhibitor and protease from P. aeruginosa was determined at 1.74 A resolution and refined to R(free) = 0.204. The structure reported here shows clearly that the N terminus of the inhibitor forms a coordinative bond to the catalytic Zn(2+) ion with a nitrogen-zinc distance of 2.17 A. We conclude that this interaction adds substantially to the complex stability and show also that similar interactions are found in other metzincin-inhibitor complexes.

PubMed: 11445573
DOI: 10.1074/JBC.M104020200

Experimental method

X-RAY DIFFRACTION (2.1 Å)