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==STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N==
==STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N==
<StructureSection load='1mjw' size='340' side='right' caption='[[1mjw]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='1mjw' size='340' side='right'caption='[[1mjw]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mjw]] is a 2 chain structure with sequence from [http://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=1MJW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MJW FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mjw]] is a 2 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=1MJW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] </span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mjw OCA], [http://pdbe.org/1mjw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mjw RCSB], [http://www.ebi.ac.uk/pdbsum/1mjw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mjw 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=1mjw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mjw OCA], [https://pdbe.org/1mjw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mjw RCSB], [https://www.ebi.ac.uk/pdbsum/1mjw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mjw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[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]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mj/1mjw_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mj/1mjw_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 18: Line 20:
</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=1mjw 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=1mjw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structures of four mutant E. coli inorganic pyrophosphatases (PPases) with single Asp--&gt;Asn substitutions at positions 42, 65, 70, and 97 were solved at 1.95, 2.15, 2.10, and 2.20 A resolution, respectively. Asp-42--&gt;Asn and Asp-65--&gt;Asn mutant PPases were prepared as complexes with sulfate--a structural analog of phosphate, the product of enzymatic reaction. A comparison of mutant enzymes with native PPases revealed that a single amino acid substitution changes the position of the mutated residue as well as the positions of several functional groups and some parts of a polypeptide chain. These changes are responsible for the fact that mutant PPases differ from the native ones in their catalytic properties. The sulfate binding to the mutant PPase active site causes molecular asymmetry, as shown for the native PPase earlier. The subunit asymmetry is manifested in different positions of sulfate and several functional groups, as well as changes in packing of hexamers in crystals and in cell parameters.


Three-dimensional structures of mutant forms of E. coli inorganic pyrophosphatase with Asp--&gt;Asn single substitution in positions 42, 65, 70, and 97.,Avaeva SM, Rodina EV, Vorobyeva NN, Kurilova SA, Nazarova TI, Sklyankina VA, Oganessyan VY, Samygina VR, Harutyunyan EH Biochemistry (Mosc). 1998 Jun;63(6):671-84. PMID:9668207<ref>PMID:9668207</ref>
==See Also==
 
*[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mjw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Inorganic diphosphatase]]
[[Category: Large Structures]]
[[Category: Avaeva, S M]]
[[Category: Avaeva SM]]
[[Category: Harutyunyan, E H]]
[[Category: Harutyunyan EH]]
[[Category: Huber, R]]
[[Category: Huber R]]
[[Category: Oganesyan, V]]
[[Category: Oganesyan V]]
[[Category: Samygina, V R]]
[[Category: Samygina VR]]
[[Category: Acid anhydride hydrolase]]
[[Category: Hydrolase]]
[[Category: Mutation]]

Latest revision as of 10:44, 14 February 2024

STRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42NSTRUCTURE OF INORGANIC PYROPHOSPHATASE MUTANT D42N

Structural highlights

1mjw is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IPYR_ECOLI

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1mjw, resolution 1.95Å

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