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| 3-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS-AERUGINOSA - A 2-DOMAIN PROTEIN WITH A CALCIUM-BINDING PARALLEL-BETA ROLL MOTIF |
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| Author(s): BAUMANN U, WU S, FLAHERTY KM, MCKAY DB |
| Source: EMBO JOURNAL Volume: 12 Issue: 9 Pages: 3357-3364 Published: SEP 1993 |
| Times Cited: 268 References: 28 |
| Abstract: The three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa, a zinc metalloprotease, has been solved to a resolution of 1.64 angstrom 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 angstrom; 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. STANFORD UNIV, MED CTR, SCH MED, DEPT CELL BIOL, BECKMAN LABS STRUCT BIOL, STANFORD, CA 94305 USA |
| Publisher: OXFORD UNIV PRESS UNITED KINGDOM, WALTON ST JOURNALS DEPT, OXFORD, ENGLAND OX2 6DP |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: LU513 |
| ISSN: 0261-4189 |
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