1jiw

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(New page: 200px<br /><applet load="1jiw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jiw, resolution 1.74&Aring;" /> '''Crystal structure of...)
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[[Image:1jiw.jpg|left|200px]]<br /><applet load="1jiw" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jiw.jpg|left|200px]]<br /><applet load="1jiw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jiw, resolution 1.74&Aring;" />
caption="1jiw, resolution 1.74&Aring;" />
'''Crystal structure of the APR-APRin complex'''<br />
'''Crystal structure of the APR-APRin complex'''<br />
==Overview==
==Overview==
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Serralysins are a family of metalloproteases secreted by Gram-negative, bacteria into the medium in the form of inactive zymogens. Usually, all, serralysin secretors have on the same operon a gene coding for a, periplasmic 10-kDa protein, which is an inhibitor of the secreted, protease. The recent characterization of the inhibitor of the alkaline, protease from Pseudomonas aeruginosa revealed a surprisingly low, dissociation constant of 4 pm, contrary to earlier studies on homologous, systems, where inhibition constants in the microm range were reported. To, approach a more accurate understanding, the crystal structure of the, complex between inhibitor and protease from P. aeruginosa was determined, at 1.74 A resolution and refined to R(free) = 0.204. The structure, reported here shows clearly that the N terminus of the inhibitor forms a, coordinative bond to the catalytic Zn(2+) ion with a nitrogen-zinc, distance of 2.17 A. We conclude that this interaction adds substantially, to the complex stability and show also that similar interactions are found, in other metzincin-inhibitor complexes.
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Serralysins are a family of metalloproteases secreted by Gram-negative bacteria into the medium in the form of inactive zymogens. Usually, all serralysin secretors have on the same operon a gene coding for a periplasmic 10-kDa protein, which is an inhibitor of the secreted protease. The recent characterization of the inhibitor of the alkaline protease from Pseudomonas aeruginosa revealed a surprisingly low dissociation constant of 4 pm, contrary to earlier studies on homologous systems, where inhibition constants in the microm range were reported. To approach a more accurate understanding, the crystal structure of the complex between inhibitor and protease from P. aeruginosa was determined at 1.74 A resolution and refined to R(free) = 0.204. The structure reported here shows clearly that the N terminus of the inhibitor forms a coordinative bond to the catalytic Zn(2+) ion with a nitrogen-zinc distance of 2.17 A. We conclude that this interaction adds substantially to the complex stability and show also that similar interactions are found in other metzincin-inhibitor complexes.
==About this Structure==
==About this Structure==
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1JIW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with ZN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JIW OCA].
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1JIW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JIW OCA].
==Reference==
==Reference==
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[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Baumann, U.]]
[[Category: Baumann, U.]]
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[[Category: Feltzer, R.E.]]
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[[Category: Feltzer, R E.]]
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[[Category: Gray, R.D.]]
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[[Category: Gray, R D.]]
[[Category: Hege, T.]]
[[Category: Hege, T.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: pseudomonas aeruginosa alkaline protease inhibitor]]
[[Category: pseudomonas aeruginosa alkaline protease inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:18:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:09 2008''

Revision as of 11:23, 21 February 2008


1jiw, resolution 1.74Å

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Crystal structure of the APR-APRin complex

Overview

Serralysins are a family of metalloproteases secreted by Gram-negative bacteria into the medium in the form of inactive zymogens. Usually, all serralysin secretors have on the same operon a gene coding for a periplasmic 10-kDa protein, which is an inhibitor of the secreted protease. The recent characterization of the inhibitor of the alkaline protease from Pseudomonas aeruginosa revealed a surprisingly low dissociation constant of 4 pm, contrary to earlier studies on homologous systems, where inhibition constants in the microm range were reported. To approach a more accurate understanding, the crystal structure of the complex between inhibitor and protease from P. aeruginosa was determined at 1.74 A resolution and refined to R(free) = 0.204. The structure reported here shows clearly that the N terminus of the inhibitor forms a coordinative bond to the catalytic Zn(2+) ion with a nitrogen-zinc distance of 2.17 A. We conclude that this interaction adds substantially to the complex stability and show also that similar interactions are found in other metzincin-inhibitor complexes.

About this Structure

1JIW is a Protein complex structure of sequences from Pseudomonas aeruginosa with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond., Hege T, Feltzer RE, Gray RD, Baumann U, J Biol Chem. 2001 Sep 14;276(37):35087-92. Epub 2001 Jul 9. PMID:11445573

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