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PDBsum entry 1kap
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Zinc metalloprotease
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PDB id
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1kap
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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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.
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Authors
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U.Baumann,
S.Wu,
K.M.Flaherty,
D.B.Mckay.
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Ref.
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Embo J, 1993,
12,
3357-3364.
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PubMed id
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Abstract
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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.
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