1KAP

THREE-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS AERUGINOSA: A TWO-DOMAIN PROTEIN WITH A CALCIUM BINDING PARALLEL BETA ROLL MOTIF

Summary for 1KAP

• Entry DOI: 10.2210/pdb1kap/pdb
• Descriptor: ALKALINE PROTEASE, TETRAPEPTIDE (GLY SER ASN SER), ZINC ION, ... (5 entities in total)
• Functional Keywords: calcium binding protein, zinc metalloprotease
• Biological source: Pseudomonas aeruginosa; More
• Cellular location: Secreted: Q03023
• Total number of polymer chains: 2
• Total formula weight: 51213.88

Authors

Baumann, U.,Wu, S.,Flaherty, K.M.,Mckay, D.B. (deposition date: 1995-06-08, release date: 1995-10-15, Last modification date: 2024-02-07)

Primary citation

Baumann, U.,Wu, S.,Flaherty, K.M.,McKay, D.B.
Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif.
EMBO J., 12:3357-3364, 1993

PubMed Abstract: The three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa, a zinc metalloprotease, has been solved to a resolution of 1.64 A by multiple isomorphous replacement and non-crystallographic symmetry averaging between different crystal forms. The molecule is elongated with overall dimensions of 90 x 35 x 25 A; it has two distinct structural domains. The N-terminal domain is the proteolytic domain; it has an overall tertiary fold and active site zinc ligation similar to that of astacin, a metalloprotease isolated from a European freshwater crayfish. The C-terminal domain consists of a 21-strand beta sandwich. Within this domain is a novel 'parallel beta roll' structure in which successive beta strands are wound in a right-handed spiral, and in which Ca2+ ions are bound within the turns between strands by a repeated GGXGXD sequence motif, a motif that is found in a diverse group of proteins secreted by Gram-negative bacteria.

PubMed: 8253063

Experimental method

X-RAY DIFFRACTION (1.64 Å)