1i40: Difference between revisions

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-[[Image:1i40.gif|left|200px]]
- {{Structure
+==STRUCTURE OF INORGANIC PYROPHOSPHATASE==
-|PDB= 1i40 |SIZE=350|CAPTION= <scene name='initialview01'>1i40</scene>, resolution 1.10&Aring;
+<StructureSection load='1i40' size='340' side='right'caption='[[1i40]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
+<table><tr><td colspan='2'>[[1i40]] 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=1I40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I40 FirstGlance]. <br>
-|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</td></tr>
-|GENE=
+<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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i40 OCA], [https://pdbe.org/1i40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i40 RCSB], [https://www.ebi.ac.uk/pdbsum/1i40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i40 ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i40 OCA], [http://www.ebi.ac.uk/pdbsum/1i40 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i40 RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/IPYR_ECOLI IPYR_ECOLI]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i4/1i40_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1i40 ConSurf].
+<div style="clear:both"></div>
-'''STRUCTURE OF INORGANIC PYROPHOSPHATASE'''
+==See Also==
+*[[Inorganic pyrophosphatase 3D structures|Inorganic pyrophosphatase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Two structures of Escherichia coli soluble inorganic pyrophosphatase (EPPase) complexed with calcium pyrophosphate (CaPP(i)-EPPase) and with Ca(2+) (Ca(2+)-EPPase) have been solved at 1.2 and 1.1 A resolution, respectively. In the presence of Mg(2+), this enzyme cleaves pyrophosphate (PP(i)) into two molecules of orthophosphate (P(i)). This work has enabled us to locate PP(i) in the active site of the inorganic pyrophosphatases family in the presence of Ca(2+), which is an inhibitor of EPPase.Upon PP(i) binding, two Ca(2+) at M1 and M2 subsites move closer together and one of the liganded water molecules becomes bridging. The mutual location of PP(i) and the bridging water molecule in the presence of inhibitor cation is catalytically incompetent. To make a favourable PP(i) attack by this water molecule, modelling of a possible hydrolysable conformation of PP(i) in the CaPP(i)-EPPase active site has been performed. The reasons for Ca(2+) being the strong PPase inhibitor and the role in catalysis of each of four metal ions are the mechanistic aspects discussed on the basis of the structures described.
-==About this Structure==
-I40 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I40 OCA].
-==Reference==
-The structures of Escherichia coli inorganic pyrophosphatase complexed with Ca(2+) or CaPP(i) at atomic resolution and their mechanistic implications., Samygina VR, Popov AN, Rodina EV, Vorobyeva NN, Lamzin VS, Polyakov KM, Kurilova SA, Nazarova TI, Avaeva SM, J Mol Biol. 2001 Nov 30;314(3):633-45. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11846572 11846572]
 [[Category: Escherichia coli]]
-[[Category: Inorganic diphosphatase]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Avaeva SM]]
-[[Category: Avaeva, S M.]]
+[[Category: Lamzin VS]]
-[[Category: Lamzin, V S.]]
+[[Category: Popov AN]]
-[[Category: Popov, A N.]]
+[[Category: Samygina VR]]
-[[Category: Samygina, V R.]]
-[[Category: calcium]]
-[[Category: hydrolase]]
-[[Category: inorganic pyrophosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:15 2008''