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==Q83S Variant of S. Enterica RmlA with dATP==
==Q83S Variant of S. Enterica RmlA with dATP==
<StructureSection load='3pkp' size='340' side='right' caption='[[3pkp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='3pkp' size='340' side='right'caption='[[3pkp]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3pkp]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PKP FirstGlance]. <br>
<table><tr><td colspan='2'>[[3pkp]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PKP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PKP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mp3|1mp3]], [[1mp4|1mp4]], [[1mp5|1mp5]], [[1iim|1iim]], [[1iin|1iin]], [[3pkq|3pkq]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DTP:2-DEOXYADENOSINE+5-TRIPHOSPHATE'>DTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rfbA, rmlA, STM2095 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</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=3pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pkp OCA], [https://pdbe.org/3pkp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pkp RCSB], [https://www.ebi.ac.uk/pdbsum/3pkp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pkp ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </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=3pkp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pkp OCA], [http://pdbe.org/3pkp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pkp RCSB], [http://www.ebi.ac.uk/pdbsum/3pkp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pkp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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> 
[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>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Directed evolution is a valuable technique to improve enzyme activity in the absence of a priori structural knowledge, which can be typically enhanced via structure-guided strategies. In this study, a combination of both whole-gene error-prone polymerase chain reaction and site-saturation mutagenesis enabled the rapid identification of mutations that improved RmlA activity toward non-native substrates. These mutations have been shown to improve activities over 10-fold for several targeted substrates, including non-native pyrimidine- and purine-based NTPs as well as non-native d- and l-sugars (both alpha- and beta-isomers). This study highlights the first broadly applicable high throughput sugar-1-phosphate nucleotidyltransferase screen and the first proof of concept for the directed evolution of this enzyme class toward the identification of uniquely permissive RmlA variants.
 
Expanding the Nucleotide and Sugar 1-Phosphate Promiscuity of Nucleotidyltransferase RmlA via Directed Evolution.,Moretti R, Chang A, Peltier-Pain P, Bingman CA, Phillips GN Jr, Thorson JS J Biol Chem. 2011 Apr 15;286(15):13235-43. Epub 2011 Feb 11. PMID:21317292<ref>PMID:21317292</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3pkp" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Glucose-1-phosphate thymidylyltransferase|Glucose-1-phosphate thymidylyltransferase]]
*[[Glucose-1-phosphate thymidylyltransferase 3D structures|Glucose-1-phosphate thymidylyltransferase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus typhimurium loeffler 1892]]
[[Category: Large Structures]]
[[Category: Glucose-1-phosphate thymidylyltransferase]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Bingman, C A]]
[[Category: Bingman CA]]
[[Category: Structural genomic]]
[[Category: Chang A]]
[[Category: Chang, A]]
[[Category: Moretti R]]
[[Category: Moretti, R]]
[[Category: Phillips Jr GN]]
[[Category: Phillips, G N]]
[[Category: Thorson JS]]
[[Category: Thorson, J S]]
[[Category: Cesg]]
[[Category: Directed evolution]]
[[Category: Nucleotidylyltransferase]]
[[Category: PSI, Protein structure initiative]]
[[Category: Transferase]]

Latest revision as of 13:41, 21 February 2024

Q83S Variant of S. Enterica RmlA with dATPQ83S Variant of S. Enterica RmlA with dATP

Structural highlights

3pkp is a 8 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.6Å
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]

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

3pkp, resolution 2.60Å

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