1ino

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Current revision (07:36, 7 February 2024) (edit) (undo)
 
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<StructureSection load='1ino' size='340' side='right'caption='[[1ino]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='1ino' size='340' side='right'caption='[[1ino]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1ino]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1INO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1ino]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1INO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1INO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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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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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] </span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ino FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ino OCA], [https://pdbe.org/1ino PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ino RCSB], [https://www.ebi.ac.uk/pdbsum/1ino PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ino ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ino FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ino OCA], [https://pdbe.org/1ino PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ino RCSB], [https://www.ebi.ac.uk/pdbsum/1ino PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ino ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IPYR_ECOLI IPYR_ECOLI]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1ino ConSurf].
</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=1ino ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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Further refinement of X-ray data on Escherichia coli inorganic pyrophosphatase [Oganessyan et al. (1994) FEBS Lett. 348, 301-304] to 2.2 A reveals a system of noncovalent interactions involving Tyr55 and Tyr141 in the active site. The pKa for one of the eight Tyr residues in wild-type pyrophosphatase is as low as 9.1 and further decreases to 8.1 upon Mg2+ binding, generating characteristic changes in the absorption spectrum. These effects are lost in a Y55F but not in a Y141F variant. It is suggested that the lower-affinity site for Mg2+ in the enzyme is formed by Tyr55 and Asp70, which are in close proximity in the apo-enzyme structure.
 
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Mg2+ activation of Escherichia coli inorganic pyrophosphatase.,Avaeva SM, Rodina EV, Kurilova SA, Nazarova TI, Vorobyeva NN, Harutyunyan EH, Oganessyan VYu FEBS Lett. 1995 Dec 11;377(1):44-6. PMID:8543015<ref>PMID:8543015</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1ino" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]]
*[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
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[[Category: Inorganic diphosphatase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Avaeva, S M]]
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[[Category: Avaeva SM]]
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[[Category: Harutyunyan, E H]]
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[[Category: Harutyunyan EH]]
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[[Category: Oganesyan, V Yu]]
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[[Category: Oganesyan VYu]]
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[[Category: Acid anhydride hydrolase]]
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[[Category: Complex]]
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[[Category: Metal binding]]
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[[Category: Mn2+ ion]]
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Current revision

RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI

PDB ID 1ino

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