1te2: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
==Putative Phosphatase Ynic from Escherichia coli K12==
==Putative Phosphatase Ynic from Escherichia coli K12==
<StructureSection load='1te2' size='340' side='right' caption='[[1te2]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
<StructureSection load='1te2' size='340' side='right'caption='[[1te2]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TE2 FirstGlance]. <br>
<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><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene><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>
<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
<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>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YNIC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 Escherichia coli O157:H7])</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=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>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoglycolate_phosphatase Phosphoglycolate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.18 3.1.3.18] </span></td></tr>
</table>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1te2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1te2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1te2 RCSB], [http://www.ebi.ac.uk/pdbsum/1te2 PDBsum], [http://www.topsan.org/Proteins/MCSG/1te2 TOPSAN]</span></td></tr>
== Function ==
<table>
[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>  
== 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/te/1te2_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/te/1te2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata 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=1te2 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli o157:h7]]
[[Category: Escherichia coli K-12]]
[[Category: Phosphoglycolate phosphatase]]
[[Category: Large Structures]]
[[Category: Edwards, A.]]
[[Category: Edwards A]]
[[Category: Evdokimova, E.]]
[[Category: Evdokimova E]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak A]]
[[Category: Kim, Y.]]
[[Category: Kim Y]]
[[Category: MCSG, Midwest Center for Structural Genomics.]]
[[Category: Savchenko A]]
[[Category: Savchenko, A.]]
[[Category: Hydrolase]]
[[Category: Mcsg]]
[[Category: Midwest center for structural genomic]]
[[Category: Phosphatase]]
[[Category: Phosphate]]
[[Category: Protein structure initiative]]
[[Category: Psi]]
[[Category: Structural genomic]]

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

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1te2&oldid=4191198"