1omj

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[[Image:1omj.jpg|left|200px]]<br /><applet load="1omj" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1omj.jpg|left|200px]]
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caption="1omj, resolution 2.38&Aring;" />
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'''CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18'''<br />
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{{Structure
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|PDB= 1omj |SIZE=350|CAPTION= <scene name='initialview01'>1omj</scene>, resolution 2.38&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1OMJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Serralysin Serralysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.40 3.4.24.40] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMJ OCA].
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1OMJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OMJ OCA].
==Reference==
==Reference==
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Probing the role of divalent metal ions in a bacterial psychrophilic metalloprotease: binding studies of an enzyme in the crystalline state by x-ray crystallography., Ravaud S, Gouet P, Haser R, Aghajari N, J Bacteriol. 2003 Jul;185(14):4195-203. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12837794 12837794]
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Probing the role of divalent metal ions in a bacterial psychrophilic metalloprotease: binding studies of an enzyme in the crystalline state by x-ray crystallography., Ravaud S, Gouet P, Haser R, Aghajari N, J Bacteriol. 2003 Jul;185(14):4195-203. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12837794 12837794]
[[Category: Pseudomonas sp.]]
[[Category: Pseudomonas sp.]]
[[Category: Serralysin]]
[[Category: Serralysin]]
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[[Category: beta jelly roll]]
[[Category: beta jelly roll]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:12:48 2008''

Revision as of 11:12, 20 March 2008

Image:1omj.jpg


PDB ID 1omj

Drag the structure with the mouse to rotate
, resolution 2.38Å
Ligands: , and
Activity: Serralysin, with EC number 3.4.24.40
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18


Overview

The psychrophilic alkaline metalloprotease (PAP) produced by a Pseudomonas bacterium isolated in Antarctica belongs to the clan of metzincins, for which a zinc ion is essential for catalytic activity. Binding studies in the crystalline state have been performed by X-ray crystallography in order to improve the understanding of the role of the zinc and calcium ions bound to this protease. Cocrystallization and soaking experiments with EDTA in a concentration range from 1 to 85 mM have resulted in five three-dimensional structures with a distinct number of metal ions occupying the ion-binding sites. Evolution of the structural changes observed in the vicinity of each cation-binding site has been studied as a function of the concentration of EDTA, as well as of time, in the presence of the chelator. Among others, we have found that the catalytic zinc ion was the first ion to be chelated, ahead of a weakly bound calcium ion (Ca 700) exclusive to the psychrophilic enzyme. Upon removal of the catalytic zinc ion, the side chains of the active-site residues His-173, His-179 and Tyr-209 shifted approximately 4, 1.0, and 1.6 A, respectively. Our studies confirm and also explain the sensitivity of PAP toward moderate EDTA concentrations and propose distinct roles for the calcium ions. A new crystal form of native PAP validates our previous predictions regarding the adaptation of this enzyme to cold environments as well as the proteolytic domain calcium ion being exclusive for PAP independent of crystallization conditions.

About this Structure

1OMJ is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

Reference

Probing the role of divalent metal ions in a bacterial psychrophilic metalloprotease: binding studies of an enzyme in the crystalline state by x-ray crystallography., Ravaud S, Gouet P, Haser R, Aghajari N, J Bacteriol. 2003 Jul;185(14):4195-203. PMID:12837794

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