1uqu

From Proteopedia

(Difference between revisions)

Current revision

Trehalose-6-phosphate from E. coli bound with UDP-glucose.

Structural highlights

1uqu is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uqu"

@@ Line 1: / Line 1: @@
-[[Image:1uqu.gif|left|200px]]<br /><applet load="1uqu" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1uqu, resolution 2.00&Aring;" />
-'''TREHALOSE-6-PHOSPHATE FROM E. COLI BOUND WITH UDP-GLUCOSE.'''<br />
-==Overview==
+==Trehalose-6-phosphate from E. coli bound with UDP-glucose.==
-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.
+<StructureSection load='1uqu' size='340' side='right'caption='[[1uqu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1uqu]] 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=1UQU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UQU 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&#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=1uqu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uqu OCA], [https://pdbe.org/1uqu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uqu RCSB], [https://www.ebi.ac.uk/pdbsum/1uqu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uqu ProSAT]</span></td></tr>
+</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 ==
+[[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/uq/1uqu_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=1uqu ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-==About this Structure==
+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<ref>PMID:14570926</ref>
-UQU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with UPG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha,alpha-trehalose-phosphate_synthase_(UDP-forming) Alpha,alpha-trehalose-phosphate synthase (UDP-forming)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.15 2.4.1.15] Known structural/functional Site: <scene name='pdbsite=AC1:Upg Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UQU OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14570926 14570926]
+</div>
-[[Category: Alpha,alpha-trehalose-phosphate synthase (UDP-forming)]]
+<div class="pdbe-citations 1uqu" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[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: UPG]]
-[[Category: glycosyltransferase]]
-[[Category: synthase]]
-[[Category: transferase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:07:29 2007''

1uqu

From Proteopedia

Current revision

Trehalose-6-phosphate from E. coli bound with UDP-glucose.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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