1qgd: Difference between revisions

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<StructureSection load='1qgd' size='340' side='right'caption='[[1qgd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1qgd' size='340' side='right'caption='[[1qgd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1qgd]] 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=1QGD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QGD FirstGlance]. <br>
<table><tr><td colspan='2'>[[1qgd]] is a 2 chain structure with sequence from [https://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=1QGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QGD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
</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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transketolase Transketolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Transketolase Transketolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.1 2.2.1.1] </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=1qgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgd OCA], [http://pdbe.org/1qgd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qgd RCSB], [http://www.ebi.ac.uk/pdbsum/1qgd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qgd 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=1qgd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgd OCA], [https://pdbe.org/1qgd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qgd RCSB], [https://www.ebi.ac.uk/pdbsum/1qgd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qgd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/TKT1_ECOLI TKT1_ECOLI]] Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.<ref>PMID:17914867</ref>   
[[https://www.uniprot.org/uniprot/TKT1_ECOLI TKT1_ECOLI]] Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.<ref>PMID:17914867</ref>   
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 12:56, 15 September 2021

TRANSKETOLASE FROM ESCHERICHIA COLITRANSKETOLASE FROM ESCHERICHIA COLI

Structural highlights

1qgd is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Transketolase, with EC number 2.2.1.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[TKT1_ECOLI] Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.[1]

Evolutionary Conservation

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

Publication Abstract from PubMed

The Escherichia coli enzyme transketolase, a dimeric protein of 2 x 70 kDa (662 amino acids) has been prepared from an overexpression system in E. coli. The purified enzyme has been crystallized from PIPES buffer pH 6.4 and ammonium sulfate. The crystals which grow as large plates diffract to greater than 1.9 A, resolution and are of the space group P2(1)2(1)2(1) with unit-cell dimensions of a = 74.6, b = 125.6 and c = 151.0 A, (Z = 8 with one transketolase dimer in the asymmetric unit). The structure has been solved by molecular replacement using the yeast transketolase enzyme structure as a search model. The enzyme is being used for large-scale biotransformations using various aldehydes and hydroxypyruvate as substrates.

Crystallization and preliminary X-ray crystallographic data with Escherichia coli transketolase.,Littlechild J, Turner N, Hobbs G, Lilly M, Rawas A, Watson H Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):1074-6. doi:, 10.1107/S0907444995005415. PMID:15299777[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Asztalos P, Parthier C, Golbik R, Kleinschmidt M, Hubner G, Weiss MS, Friedemann R, Wille G, Tittmann K. Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry. 2007 Oct 30;46(43):12037-52. Epub 2007 Oct 3. PMID:17914867 doi:10.1021/bi700844m
  2. ↑ Littlechild J, Turner N, Hobbs G, Lilly M, Rawas A, Watson H. Crystallization and preliminary X-ray crystallographic data with Escherichia coli transketolase. Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):1074-6. doi:, 10.1107/S0907444995005415. PMID:15299777 doi:http://dx.doi.org/10.1107/S0907444995005415

1qgd, resolution 1.90Å

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