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| | <StructureSection load='1uqt' size='340' side='right'caption='[[1uqt]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='1uqt' size='340' side='right'caption='[[1uqt]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1uqt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UQT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1uqt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UQT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UQT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=U2F:URIDINE-5-DIPHOSPHATE-2-DEOXY-2-FLUORO-ALPHA-D-GLUCOSE'>U2F</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]] 2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gz5|1gz5]], [[1uqu|1uqu]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=U2F:URIDINE-5-DIPHOSPHATE-2-DEOXY-2-FLUORO-ALPHA-D-GLUCOSE'>U2F</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha,alpha-trehalose-phosphate_synthase_(UDP-forming) Alpha,alpha-trehalose-phosphate synthase (UDP-forming)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.15 2.4.1.15] </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=1uqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqt OCA], [https://pdbe.org/1uqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uqt RCSB], [https://www.ebi.ac.uk/pdbsum/1uqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uqt 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=1uqt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqt OCA], [https://pdbe.org/1uqt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uqt RCSB], [https://www.ebi.ac.uk/pdbsum/1uqt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uqt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/OTSA_ECOLI OTSA_ECOLI] Catalyzes the transfer of glucose from UDP-glucose to glucose-6-phosphate to form alpha,alpha-1,1 trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor. Essential for viability of the cells at low temperatures and at elevated osmotic strength.<ref>PMID:1310094</ref> <ref>PMID:3131312</ref> <ref>PMID:12105274</ref> |
| | == 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: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Davies, G J]] | + | [[Category: Davies GJ]] |
| - | [[Category: Gibson, R P]] | + | [[Category: Gibson RP]] |
| - | [[Category: Roberts, S]] | + | [[Category: Roberts S]] |
| - | [[Category: Tarling, C A]] | + | [[Category: Tarling CA]] |
| - | [[Category: Withers, S G]] | + | [[Category: Withers SG]] |
| - | [[Category: Glycosyltransferase]]
| + | |
| - | [[Category: Synthase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
OTSA_ECOLI Catalyzes the transfer of glucose from UDP-glucose to glucose-6-phosphate to form alpha,alpha-1,1 trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor. Essential for viability of the cells at low temperatures and at elevated osmotic strength.[1] [2] [3]
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
Trehalose is an unusual non-reducing disaccharide that plays a variety of biological roles, from food storage to cellular protection from environmental stresses such as desiccation, pressure, heat-shock, extreme cold, and oxygen radicals. It is also an integral component of the cell-wall glycolipids of mycobacteria. The primary enzymatic route to trehalose first involves the transfer of glucose from a UDP-glucose donor to glucose-6-phosphate to form alpha,alpha-1,1 trehalose-6-phosphate. This reaction, in which the configurations of two glycosidic bonds are set simultaneously, is catalyzed by the glycosyltransferase trehalose-6-phosphate synthase (OtsA), which acts with retention of the anomeric configuration of the UDP-sugar donor. The classification of activated sugar-dependent glycosyltransferases into approximately 70 distinct families based upon amino acid sequence similarities places OtsA in glycosyltransferase family 20 (see afmb.cnrs-mrs.fr/CAZY/). The recent 2.4 A structure of Escherichia coli OtsA revealed a two-domain enzyme with catalysis occurring at the interface of the twin beta/alpha/beta domains. Here we present the 2.0 A structures of the E. coli OtsA in complex with either UDP-Glc or the non-transferable analogue UDP-2-deoxy-2-fluoroglucose. Both complexes unveil the donor subsite interactions, confirming a strong similarity to glycogen phosphorylases, and reveal substantial conformational differences to the previously reported complex with UDP and glucose 6-phosphate. Both the relative orientation of the two domains and substantial (up to 10 A) movements of an N-terminal loop (residues 9-22) characterize the more open "relaxed" conformation of the binary UDP-sugar complexes reported here.
The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution.,Gibson RP, Tarling CA, Roberts S, Withers SG, Davies GJ J Biol Chem. 2004 Jan 16;279(3):1950-5. Epub 2003 Oct 21. PMID:14570926[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kaasen I, Falkenberg P, Styrvold OB, Strom AR. Molecular cloning and physical mapping of the otsBA genes, which encode the osmoregulatory trehalose pathway of Escherichia coli: evidence that transcription is activated by katF (AppR) J Bacteriol. 1992 Feb;174(3):889-98. PMID:1310094
- ↑ Giaever HM, Styrvold OB, Kaasen I, Strom AR. Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli. J Bacteriol. 1988 Jun;170(6):2841-9. PMID:3131312
- ↑ Kandror O, DeLeon A, Goldberg AL. Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures. Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9727-32. Epub 2002 Jul 8. PMID:12105274 doi:http://dx.doi.org/10.1073/pnas.142314099
- ↑ Gibson RP, Tarling CA, Roberts S, Withers SG, Davies GJ. The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution. J Biol Chem. 2004 Jan 16;279(3):1950-5. Epub 2003 Oct 21. PMID:14570926 doi:10.1074/jbc.M307643200
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