1qgd: Difference between revisions

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[[Image:1qgd.jpg|left|200px]]


{{Structure
==TRANSKETOLASE FROM ESCHERICHIA COLI==
|PDB= 1qgd |SIZE=350|CAPTION= <scene name='initialview01'>1qgd</scene>, resolution 1.9&Aring;
<StructureSection load='1qgd' size='340' side='right'caption='[[1qgd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</scene>
<table><tr><td colspan='2'>[[1qgd]] is a 2 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=1QGD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QGD FirstGlance]. <br>
|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TPP:THIAMINE+DIPHOSPHATE'>TPP</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=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>
|RELATEDENTRY=
</table>
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1qgd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qgd RCSB]</span>
== Function ==
}}
[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 ==
[[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/qg/1qgd_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=1qgd ConSurf].
<div style="clear:both"></div>


'''TRANSKETOLASE FROM ESCHERICHIA COLI'''
==See Also==
 
*[[Transketolase 3D structures|Transketolase 3D structures]]
 
== References ==
==About this Structure==
<references/>
1QGD 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=1QGD OCA].
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Transketolase]]
[[Category: Isupov MN]]
[[Category: Isupov, M N.]]
[[Category: Littlechild JA]]
[[Category: Littlechild, J A.]]
[[Category: d-sedoheptulose 7-phosphate d-glyceraldehyde 3- phosphate glycolaldehyde transferase]]
[[Category: thiamine pyrophosphate]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:13:12 2008''

Latest revision as of 13:02, 16 August 2023

TRANSKETOLASE FROM ESCHERICHIA COLITRANSKETOLASE FROM ESCHERICHIA COLI

Structural highlights

1qgd is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, ,
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.

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

1qgd, resolution 1.90Å

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