1ezm: Difference between revisions
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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[[Image:1ezm.gif|left|200px]]<br /><applet load="1ezm" size=" | [[Image:1ezm.gif|left|200px]]<br /><applet load="1ezm" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ezm, resolution 1.5Å" /> | caption="1ezm, resolution 1.5Å" /> | ||
'''THREE-DIMENSIONAL STRUCTURE OF THE ELASTASE OF PSEUDOMONAS AERUGINOSA AT 1.5 ANGSTROMS RESOLUTION'''<br /> | '''THREE-DIMENSIONAL STRUCTURE OF THE ELASTASE OF PSEUDOMONAS AERUGINOSA AT 1.5 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
Pseudomonas aeruginosa elastase (PAE) is a zinc metalloprotease with 301 | 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 Structure== | ==About this Structure== | ||
1EZM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pseudolysin Pseudolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.26 3.4.24.26] Full crystallographic information is available from [http:// | 1EZM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pseudolysin Pseudolysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.26 3.4.24.26] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EZM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Pseudolysin]] | [[Category: Pseudolysin]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Flaherty, K | [[Category: Flaherty, K M.]] | ||
[[Category: Mckay, D | [[Category: Mckay, D B.]] | ||
[[Category: Thayer, M | [[Category: Thayer, M M.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:33:14 2008'' |
Revision as of 13:33, 21 February 2008
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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 and 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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