1iin: Difference between revisions

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


{{Structure
==thymidylyltransferase complexed with UDP-glucose==
|PDB= 1iin |SIZE=350|CAPTION= <scene name='initialview01'>1iin</scene>, resolution 2.10&Aring;
<StructureSection load='1iin' size='340' side='right'caption='[[1iin]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=UPG:URIDINE-5'-DIPHOSPHATE-GLUCOSE'>UPG</scene>
<table><tr><td colspan='2'>[[1iin]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IIN FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Glucose-1-phosphate_thymidylyltransferase Glucose-1-phosphate thymidylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.24 2.7.7.24]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</scene></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=1iin FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iin OCA], [https://pdbe.org/1iin PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iin RCSB], [https://www.ebi.ac.uk/pdbsum/1iin PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iin ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RMLA_SALTY RMLA_SALTY] Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is also able to convert non natural substrates such as a wide array of alpha-D-hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy-alpha-D-hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars.<ref>PMID:8382158</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/ii/1iin_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=1iin ConSurf].
<div style="clear:both"></div>


'''thymidylyltransferase complexed with UDP-glucose'''
==See Also==
 
*[[Glucose-1-phosphate thymidylyltransferase 3D structures|Glucose-1-phosphate thymidylyltransferase 3D structures]]
 
== References ==
==Overview==
<references/>
Metabolite glycosylation is affected by three classes of enzymes: nucleotidylyltransferases, which activate sugars as nucleotide diphospho-derivatives, intermediate sugar-modifying enzymes and glycosyltransferases, which transfer the final derivatized activated sugars to aglycon substrates. One of the first crystal structures of an enzyme responsible for the first step in this cascade, alpha-D-glucopyranosyl phosphate thymidylyltransferase (Ep) from Salmonella, in complex with product (UDP-Glc) and substrate (dTTP) is reported at 2.0 A and 2.1 A resolution, respectively. These structures, in conjunction with the kinetic characterization of Ep, clarify the catalytic mechanism of this important enzyme class. Structure-based engineering of Ep produced modified enzymes capable of utilizing 'unnatural' sugar phosphates not accepted by wild type Ep. The demonstrated ability to alter nucleotidylyltransferase specificity by design is an integral component of in vitro glycosylation systems developed for the production of diverse glycorandomized libraries.
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1IIN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IIN OCA].
 
==Reference==
Structure, mechanism and engineering of a nucleotidylyltransferase as a first step toward glycorandomization., Barton WA, Lesniak J, Biggins JB, Jeffrey PD, Jiang J, Rajashankar KR, Thorson JS, Nikolov DB, Nat Struct Biol. 2001 Jun;8(6):545-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11373625 11373625]
[[Category: Glucose-1-phosphate thymidylyltransferase]]
[[Category: Salmonella enterica]]
[[Category: Salmonella enterica]]
[[Category: Single protein]]
[[Category: Barton WA]]
[[Category: Barton, W A.]]
[[Category: Biggins JB]]
[[Category: Biggins, J B.]]
[[Category: Jeffrey PD]]
[[Category: Jeffrey, P D.]]
[[Category: Jiang J]]
[[Category: Jiang, J.]]
[[Category: Lesniak J]]
[[Category: Lesniak, J.]]
[[Category: Nikolov DB]]
[[Category: Nikolov, D B.]]
[[Category: Rajashankar KR]]
[[Category: Rajashankar, K R.]]
[[Category: Thorson JS]]
[[Category: Thorson, J S.]]
[[Category: UPG]]
[[Category: transferase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:50:56 2008''

Latest revision as of 10:36, 7 February 2024

thymidylyltransferase complexed with UDP-glucosethymidylyltransferase complexed with UDP-glucose

Structural highlights

1iin is a 4 chain structure with sequence from Salmonella enterica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RMLA_SALTY Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. Is also able to convert non natural substrates such as a wide array of alpha-D-hexopyranosyl, deoxy-alpha-D-glucopyranosyl, aminodeoxy-alpha-D-hexopyranosyl and acetamidodeoxy-alpha-D-hexopyranosyl phosphates to their corresponding dTDP- and UDP-nucleotide sugars.[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. ↑ Lindquist L, Kaiser R, Reeves PR, Lindberg AA. Purification, characterization and HPLC assay of Salmonella glucose-1-phosphate thymidylyl-transferase from the cloned rfbA gene. Eur J Biochem. 1993 Feb 1;211(3):763-70. PMID:8382158

1iin, resolution 2.10Å

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