1kap
From Proteopedia
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THREE-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS AERUGINOSA: A TWO-DOMAIN PROTEIN WITH A CALCIUM BINDING PARALLEL BETA ROLL MOTIF
Overview
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.
About this Structure
1KAP is a Single protein structure of sequence from Pseudomonas aeruginosa with ZN and CA as ligands. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif., Baumann U, Wu S, Flaherty KM, McKay DB, EMBO J. 1993 Sep;12(9):3357-64. PMID:8253063
Page seeded by OCA on Tue Nov 20 19:00:22 2007
