1mp4: Difference between revisions

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New page: left|200px<br /><applet load="1mp4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mp4, resolution 2.20Å" /> '''W224H VARIANT OF S. ...
 
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'''W224H VARIANT OF S. ENTERICA RmlA'''<br />


==Overview==
==W224H VARIANT OF S. ENTERICA RmlA==
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.
<StructureSection load='1mp4' size='340' side='right'caption='[[1mp4]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mp4]] is a 2 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=1MP4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MP4 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mp4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mp4 OCA], [https://pdbe.org/1mp4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mp4 RCSB], [https://www.ebi.ac.uk/pdbsum/1mp4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mp4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9F7G8_SALER Q9F7G8_SALER] Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.[RuleBase:RU003706]
== 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/mp/1mp4_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=1mp4 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MP4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Salmonella_enterica Salmonella enterica] with UPG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MP4 OCA].
*[[Glucose-1-phosphate thymidylyltransferase 3D structures|Glucose-1-phosphate thymidylyltransferase 3D structures]]
 
*[[Tumor susceptibility gene 101|Tumor susceptibility gene 101]]
==Reference==
__TOC__
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12374866 12374866]
</StructureSection>
[[Category: Glucose-1-phosphate thymidylyltransferase]]
[[Category: Large Structures]]
[[Category: Salmonella enterica]]
[[Category: Salmonella enterica]]
[[Category: Single protein]]
[[Category: Barton WA]]
[[Category: Barton, W.A.]]
[[Category: Biggins JB]]
[[Category: Biggins, J.B.]]
[[Category: Jiang J]]
[[Category: Jiang, J.]]
[[Category: Nikolov DB]]
[[Category: Nikolov, D.B.]]
[[Category: Thorson JS]]
[[Category: Thorson, J.S.]]
[[Category: UPG]]
[[Category: transferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 21:46:39 2007''

Latest revision as of 10:46, 14 February 2024

W224H VARIANT OF S. ENTERICA RmlAW224H VARIANT OF S. ENTERICA RmlA

Structural highlights

1mp4 is a 2 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 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q9F7G8_SALER Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis.[RuleBase:RU003706]

Evolutionary Conservation

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

See Also

1mp4, resolution 2.20Å

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