2b0c: Difference between revisions

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==The crystal structure of the putative phosphatase from Escherichia coli==
==The crystal structure of the putative phosphatase from Escherichia coli==
<StructureSection load='2b0c' size='340' side='right' caption='[[2b0c]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2b0c' size='340' side='right' caption='[[2b0c]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G1P:ALPHA-D-GLUCOSE-1-PHOSPHATE'>G1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G1P:ALPHA-D-GLUCOSE-1-PHOSPHATE'>G1P</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yihX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">yihX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=2b0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b0c OCA], [http://pdbe.org/2b0c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b0c RCSB], [http://www.ebi.ac.uk/pdbsum/2b0c PDBsum], [http://www.topsan.org/Proteins/MCSG/2b0c TOPSAN]</span></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=2b0c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b0c OCA], [http://pdbe.org/2b0c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b0c RCSB], [http://www.ebi.ac.uk/pdbsum/2b0c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b0c ProSAT], [http://www.topsan.org/Proteins/MCSG/2b0c TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b0/2b0c_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b0/2b0c_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>

Revision as of 09:33, 16 May 2018

The crystal structure of the putative phosphatase from Escherichia coliThe crystal structure of the putative phosphatase from Escherichia coli

Structural highlights

2b0c is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Gene:yihX (ECOLI)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[YIHX_ECOLI] Catalyzes the dephosphorylation of alpha-D-glucose-1-phosphate (Glu1P) and has no activity with the beta form. In addition, YihX has phosphatase activity against sugar-phosphate and pyridoxal phosphate (PLP) and low beta-phosphoglucomutase activity.[1] [2]

Evolutionary Conservation

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

References

  1. ↑ Kuznetsova E, Proudfoot M, Sanders SA, Reinking J, Savchenko A, Arrowsmith CH, Edwards AM, Yakunin AF. Enzyme genomics: Application of general enzymatic screens to discover new enzymes. FEMS Microbiol Rev. 2005 Apr;29(2):263-79. PMID:15808744 doi:S0168-6445(05)00004-5
  2. ↑ Kuznetsova E, Proudfoot M, Gonzalez CF, Brown G, Omelchenko MV, Borozan I, Carmel L, Wolf YI, Mori H, Savchenko AV, Arrowsmith CH, Koonin EV, Edwards AM, Yakunin AF. Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J Biol Chem. 2006 Nov 24;281(47):36149-61. Epub 2006 Sep 21. PMID:16990279 doi:10.1074/jbc.M605449200

2b0c, resolution 2.00Å

Drag the structure with the mouse to rotate

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