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==Y177F VARIANT OF S. ENTERICA RmlA==
==Y177F VARIANT OF S. ENTERICA RmlA==
<StructureSection load='1mp5' size='340' side='right' caption='[[1mp5]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
<StructureSection load='1mp5' size='340' side='right'caption='[[1mp5]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mp5]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_cholerae-suis"_smith_1894 "bacillus cholerae-suis" smith 1894]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MP5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MP5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mp5]] 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=1MP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MP5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UPG:URIDINE-5-DIPHOSPHATE-GLUCOSE'>UPG</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]] 2.75&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1iim|1iim]], [[1iin|1iin]], [[1mp3|1mp3]], [[1mp4|1mp4]]</td></tr>
<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='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'>[https://proteopedia.org/fgij/fg.htm?mol=1mp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp5 OCA], [https://pdbe.org/1mp5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mp5 RCSB], [https://www.ebi.ac.uk/pdbsum/1mp5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mp5 ProSAT]</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=1mp5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp5 OCA], [http://pdbe.org/1mp5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mp5 RCSB], [http://www.ebi.ac.uk/pdbsum/1mp5 PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q9F7G8_SALCE Q9F7G8_SALCE]] Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.[RuleBase:RU003706]
[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 ==
== 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/mp/1mp5_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mp/1mp5_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 20: Line 20:
</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=1mp5 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=1mp5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In vitro "glycorandomization" is a chemoenzymatic approach for generating diverse libraries of glycosylated biomolecules based on natural product scaffolds. This technology makes use of engineered variants of specific enzymes affecting metabolite glycosylation, particularly nucleotidylyltransferases and glycosyltransferases. To expand the repertoire of UDP/dTDP sugars readily available for glycorandomization, we now report a structure-based engineering approach to increase the diversity of alpha-d-hexopyranosyl phosphates accepted by Salmonella enterica LT2 alpha-d-glucopyranosyl phosphate thymidylyltransferase (E(p)). This article highlights the design rationale, determined substrate specificity, and structural elucidation of three "designed" mutations, illustrating both the success and unexpected outcomes from this type of approach. In addition, a single amino acid substitution in the substrate-binding pocket (L89T) was found to significantly increase the set of alpha-d-hexopyranosyl phosphates accepted by E(p) to include alpha-d-allo-, alpha-d-altro-, and alpha-d-talopyranosyl phosphate. In aggregate, our results provide valuable blueprints for altering nucleotidylyltransferase specificity by design, which is the first step toward in vitro glycorandomization.
Expanding pyrimidine diphosphosugar libraries via structure-based nucleotidylyltransferase engineering.,Barton WA, Biggins JB, Jiang J, Thorson JS, Nikolov DB Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13397-402. Epub 2002 Oct 8. PMID:12374866<ref>PMID:12374866</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mp5" 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 cholerae-suis smith 1894]]
[[Category: Large Structures]]
[[Category: Glucose-1-phosphate thymidylyltransferase]]
[[Category: Salmonella enterica]]
[[Category: Barton, W A]]
[[Category: Barton WA]]
[[Category: Biggins, J B]]
[[Category: Biggins JB]]
[[Category: Jiang, J]]
[[Category: Jiang J]]
[[Category: Nikolov, D B]]
[[Category: Nikolov DB]]
[[Category: Thorson, J S]]
[[Category: Thorson JS]]
[[Category: Transferase]]

Latest revision as of 10:46, 14 February 2024

Y177F VARIANT OF S. ENTERICA RmlAY177F VARIANT OF S. ENTERICA RmlA

Structural highlights

1mp5 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 2.75Å
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

1mp5, resolution 2.75Å

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