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1o0q

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[[Image:1o0q.gif|left|200px]]
 
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{{Structure
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==Crystal structure of a cold adapted alkaline protease from Pseudomonas TAC II 18, co-crystallized with 1 mM EDTA==
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|PDB= 1o0q |SIZE=350|CAPTION= <scene name='initialview01'>1o0q</scene>, resolution 2.2&Aring;
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<StructureSection load='1o0q' size='340' side='right'caption='[[1o0q]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1o0q]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._'TAC_II_18' Pseudomonas sp. 'TAC II 18']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O0Q FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0q OCA], [https://pdbe.org/1o0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o0q RCSB], [https://www.ebi.ac.uk/pdbsum/1o0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o0q ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1g9k|1G9K]], [[1h71|1H71]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o0q OCA], [http://www.ebi.ac.uk/pdbsum/1o0q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o0q RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/O69771_9PSED O69771_9PSED]
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== Evolutionary Conservation ==
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'''Crystal structure of a cold adapted alkaline protease from Pseudomonas TAC II 18, co-crystallized with 1 mM EDTA'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o0/1o0q_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1O0Q 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=1O0Q OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o0q ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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]
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</StructureSection>
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[[Category: Pseudomonas sp.]]
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[[Category: Large Structures]]
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[[Category: Serralysin]]
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[[Category: Pseudomonas sp. 'TAC II 18']]
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[[Category: Single protein]]
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[[Category: Aghajari N]]
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[[Category: Aghajari, N.]]
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[[Category: Gouet P]]
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[[Category: Gouet, P.]]
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[[Category: Haser R]]
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[[Category: Haser, R.]]
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[[Category: Ravaud S]]
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[[Category: Ravaud, S.]]
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[[Category: beta jelly roll]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:38:10 2008''
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Current revision

Crystal structure of a cold adapted alkaline protease from Pseudomonas TAC II 18, co-crystallized with 1 mM EDTA

PDB ID 1o0q

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