1gz5

From Proteopedia

(Difference between revisions)

Revision as of 11:04, 31 March 2021

Trehalose-6-phosphate synthase. OtsA

Structural highlights

1gz5 is a 4 chain structure with sequence from Ecow3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Activity:	Alpha,alpha-trehalose-phosphate synthase (UDP-forming), with EC number 2.4.1.15
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 a nonreducing disaccharide that plays a major role in many organisms, most notably in survival and stress responses. In Mycobacterium tuberculosis, it plays a central role as the carbohydrate core of numerous immunogenic glycolipids including "cord factor" (trehalose 6,6'-dimycolate). The classical pathway for trehalose synthesis involves the condensation of UDP-glucose and glucose-6-phosphate to afford trehalose-6-phosphate, catalyzed by the retaining glycosyltransferase OtsA. The configurations of two anomeric positions are set simultaneously, resulting in the formation of a double glycoside. The three-dimensional structure of the Escherichia coli OtsA, in complex with both UDP and glucose-6-phosphate, reveals the active site at the interface of two beta/alpha/beta domains. The overall structure and the intimate details of the catalytic machinery reveal a striking similarity to glycogen phosphorylase, indicating a strong evolutionary link and suggesting a common catalytic mechanism.

Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA.,Gibson RP, Turkenburg JP, Charnock SJ, Lloyd R, Davies GJ Chem Biol. 2002 Dec;9(12):1337-46. PMID:12498887^[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, Turkenburg JP, Charnock SJ, Lloyd R, Davies GJ. Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA. Chem Biol. 2002 Dec;9(12):1337-46. PMID:12498887

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/1gz5"

@@ Line 3: / Line 3: @@
 <StructureSection load='1gz5' size='340' side='right'caption='[[1gz5]], [[Resolution|resolution]] 2.43&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1gz5]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GZ5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1gz5]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecow3 Ecow3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GZ5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=UDP:URIDINE-5-DIPHOSPHATE'>UDP</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gz5 OCA], [http://pdbe.org/1gz5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gz5 RCSB], [http://www.ebi.ac.uk/pdbsum/1gz5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gz5 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=1gz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gz5 OCA], [https://pdbe.org/1gz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gz5 RCSB], [https://www.ebi.ac.uk/pdbsum/1gz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gz5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[[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]]
@@ Line 34: / Line 34: @@
 __TOC__
 </StructureSection>
+[[Category: Ecow3]]
 [[Category: Large Structures]]
 [[Category: Davies, G J]]

1gz5

From Proteopedia

Revision as of 11:04, 31 March 2021

Trehalose-6-phosphate synthase. OtsA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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