1ezm: Difference between revisions

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[[Image:1ezm.gif|left|200px]]
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{{STRUCTURE_1ezm|  PDB=1ezm  |  SCENE=  }}  
{{STRUCTURE_1ezm|  PDB=1ezm  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_1899664}}


==About this Structure==
==About this Structure==
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[[Category: Thayer, M M.]]
[[Category: Thayer, M M.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
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Revision as of 02:15, 1 July 2008

File:1ezm.png

Template:STRUCTURE 1ezm

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

Template:ABSTRACT PUBMED 1899664

About this StructureAbout this Structure

1EZM is a Single protein structure. 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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