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| | <StructureSection load='2ux8' size='340' side='right'caption='[[2ux8]], [[Resolution|resolution]] 2.65Å' scene=''> | | <StructureSection load='2ux8' size='340' side='right'caption='[[2ux8]], [[Resolution|resolution]] 2.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ux8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"pseudomonas_elodea"_kang_et_al._1982 "pseudomonas elodea" kang et al. 1982]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UX8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2UX8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ux8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_elodea Sphingomonas elodea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2UX8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2UX8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G1P:ALPHA-D-GLUCOSE-1-PHOSPHATE'>G1P</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]] 2.65Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UTP--glucose-1-phosphate_uridylyltransferase UTP--glucose-1-phosphate uridylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.9 2.7.7.9] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G1P:ALPHA-D-GLUCOSE-1-PHOSPHATE'>G1P</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2ux8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ux8 OCA], [http://pdbe.org/2ux8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ux8 RCSB], [http://www.ebi.ac.uk/pdbsum/2ux8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ux8 ProSAT]</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=2ux8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ux8 OCA], [https://pdbe.org/2ux8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ux8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ux8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ux8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5FYV5_SPHEL Q5FYV5_SPHEL] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Pseudomonas elodea kang et al. 1982]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: UTP--glucose-1-phosphate uridylyltransferase]] | + | [[Category: Sphingomonas elodea]] |
| - | [[Category: Aragao, D]] | + | [[Category: Aragao D]] |
| - | [[Category: Fialho, A M]] | + | [[Category: Fialho AM]] |
| - | [[Category: Frazao, C]] | + | [[Category: Frazao C]] |
| - | [[Category: Marques, A R]] | + | [[Category: Marques AR]] |
| - | [[Category: Mitchell, E P]] | + | [[Category: Mitchell EP]] |
| - | [[Category: Sa-Correia, I]] | + | [[Category: Sa-Correia I]] |
| - | [[Category: Galu pyrophosphorylase]]
| + | |
| - | [[Category: Glucose-1-phosphate uridylyltransferase]]
| + | |
| - | [[Category: Nucleotidyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| - | [[Category: Ugpg]]
| + | |
| Structural highlights
Function
Q5FYV5_SPHEL
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Gellan gum is a widely used commercial material, available in many different forms. Its economic importance has led to studies into the biosynthesis of exopolysaccharide gellan gum, which is industrially prepared in high yields using Sphingomonas elodea ATCC 31461. Glucose-1-phosphate uridylyltransferase mediates the reversible conversion of glucose-1-phosphate and UTP into UDP-glucose and pyrophosphate, which is a key step in the biosynthetic pathway of gellan gums. Here we present the X-ray crystal structure of the glucose-1-phosphate uridylyltransferase from S. elodea. The S. elodea enzyme shares strong monomeric similarity with glucose-1-phosphate thymidylyltransferase, several structures of which are known, although the quaternary structures of the active enzymes are rather different. A detailed comparison between S. elodea glucose-1-phosphate uridylyltransferase and available thymidylyltransferases is described and shows remarkable structural similarities, despite the low sequence identities between the two divergent groups of proteins.
The complex of Sphingomonas elodea ATCC 31461 glucose-1-phosphate uridylyltransferase with glucose-1-phosphate reveals a novel quaternary structure, unique among nucleoside diphosphate-sugar pyrophosphorylase members.,Aragao D, Fialho AM, Marques AR, Mitchell EP, Sa-Correia I, Frazao C J Bacteriol. 2007 Jun;189(12):4520-8. Epub 2007 Apr 13. PMID:17434970[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Aragao D, Fialho AM, Marques AR, Mitchell EP, Sa-Correia I, Frazao C. The complex of Sphingomonas elodea ATCC 31461 glucose-1-phosphate uridylyltransferase with glucose-1-phosphate reveals a novel quaternary structure, unique among nucleoside diphosphate-sugar pyrophosphorylase members. J Bacteriol. 2007 Jun;189(12):4520-8. Epub 2007 Apr 13. PMID:17434970 doi:http://dx.doi.org/10.1128/JB.00277-07
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