1te2: Difference between revisions

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[[Image:1te2.png|left|200px]]


{{STRUCTURE_1te2|  PDB=1te2  |  SCENE=  }}
==Putative Phosphatase Ynic from Escherichia coli K12==
 
<StructureSection load='1te2' size='340' side='right'caption='[[1te2]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
===Putative Phosphatase Ynic from Escherichia coli K12===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1te2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TE2 FirstGlance]. <br>
 
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
==About this Structure==
<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=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
[[1te2]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_o157:h7 Escherichia coli o157:h7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TE2 OCA].  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1te2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1te2 OCA], [https://pdbe.org/1te2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1te2 RCSB], [https://www.ebi.ac.uk/pdbsum/1te2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1te2 ProSAT], [https://www.topsan.org/Proteins/MCSG/1te2 TOPSAN]</span></td></tr>
[[Category: Escherichia coli o157:h7]]
</table>
[[Category: Phosphoglycolate phosphatase]]
== Function ==
[[Category: Edwards, A.]]
[https://www.uniprot.org/uniprot/HXPB_ECOLI HXPB_ECOLI] Sugar-phosphate phosphohydrolase that catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate (PubMed:27941785). Also catalyzes the dephosphorylation of 2-deoxyglucose 6-phosphate (2dGlu6P); this is a biologically important activity in vivo since it contributes to the elimination of this toxic compound and plays an important role in the resistance of E.coli to 2-deoxyglucose (PubMed:16990279). To a lesser extent, is also able to dephosphorylate mannose 6-phosphate (Man6P), erythrose-4-phosphate, 2-deoxyribose-5-phosphate (2dRib5P), ribose-5-phosphate (Rib5P) and glucose-6-phosphate (Glu6P) in vitro (PubMed:16990279).<ref>PMID:15808744</ref> <ref>PMID:16990279</ref> <ref>PMID:27941785</ref>
[[Category: Evdokimova, E.]]
== Evolutionary Conservation ==
[[Category: Joachimiak, A.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Kim, Y.]]
Check<jmol>
[[Category: MCSG, Midwest Center for Structural Genomics.]]
  <jmolCheckbox>
[[Category: Savchenko, A.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/te/1te2_consurf.spt"</scriptWhenChecked>
[[Category: Hydrolase]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
[[Category: Mcsg]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Midwest center for structural genomic]]
  </jmolCheckbox>
[[Category: Phosphatase]]
</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=1te2 ConSurf].
[[Category: Phosphate]]
<div style="clear:both"></div>
[[Category: Protein structure initiative]]
== References ==
[[Category: Psi]]
<references/>
[[Category: Structural genomic]]
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Edwards A]]
[[Category: Evdokimova E]]
[[Category: Joachimiak A]]
[[Category: Kim Y]]
[[Category: Savchenko A]]

Latest revision as of 07:54, 17 October 2024

Putative Phosphatase Ynic from Escherichia coli K12Putative Phosphatase Ynic from Escherichia coli K12

Structural highlights

1te2 is a 2 chain structure with sequence from Escherichia coli K-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.76Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

HXPB_ECOLI Sugar-phosphate phosphohydrolase that catalyzes the dephosphorylation of D-mannitol 1-phosphate and D-sorbitol 6-phosphate (PubMed:27941785). Also catalyzes the dephosphorylation of 2-deoxyglucose 6-phosphate (2dGlu6P); this is a biologically important activity in vivo since it contributes to the elimination of this toxic compound and plays an important role in the resistance of E.coli to 2-deoxyglucose (PubMed:16990279). To a lesser extent, is also able to dephosphorylate mannose 6-phosphate (Man6P), erythrose-4-phosphate, 2-deoxyribose-5-phosphate (2dRib5P), ribose-5-phosphate (Rib5P) and glucose-6-phosphate (Glu6P) in vitro (PubMed:16990279).[1] [2] [3]

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
  3. ↑ Sevin DC, Fuhrer T, Zamboni N, Sauer U. Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli. Nat Methods. 2017 Feb;14(2):187-194. doi: 10.1038/nmeth.4103. Epub 2016 Dec 12. PMID:27941785 doi:http://dx.doi.org/10.1038/nmeth.4103

1te2, resolution 1.76Å

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