1ezm

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Revision as of 15:21, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1ezm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ezm, resolution 1.5Å" /> '''THREE-DIMENSIONAL STR...)
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File:1ezm.gif


1ezm, resolution 1.5Å

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THREE-DIMENSIONAL STRUCTURE OF THE ELASTASE OF PSEUDOMONAS AERUGINOSA AT 1.5 ANGSTROMS RESOLUTION

OverviewOverview

Pseudomonas aeruginosa elastase (PAE) is a zinc metalloprotease with 301, amino acids. We have crystallized and solved the three-dimensional, structure of PAE, using data to 1.5-A resolution, and have refined the, native molecular structure to R = 0.188. The overall tertiary structure of, the PAE molecule is similar to that of thermolysin, with which it shares, 28% amino acid sequence identity. Nearly all of the active site residues, that might potentially interact with substrates are identical in the two, proteins. However, the active site cleft is significantly more "open" in, PAE than in thermolysin.

About this StructureAbout this Structure

1EZM is a Single protein structure of sequence from [1] with ZN and CA as ligands. Active as Pseudolysin, with EC number 3.4.24.26 Full crystallographic information is available from OCA.

ReferenceReference

Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution., Thayer MM, Flaherty KM, McKay DB, J Biol Chem. 1991 Feb 15;266(5):2864-71. PMID:1899664

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