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6jak

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OtsA apo structure

Structural highlights

6jak is a 4 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 2.41Å
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]

Publication Abstract from PubMed

Trehalose-6-phosphate (T6P) synthase (Tps1) catalyzes the formation of T6P from UDP-glucose (UDPG) (or GDPG, etc.) and glucose-6-phosphate (G6P), and structural basis of this process has not been well studied. MoTps1 (Magnaporthe oryzae Tps1) plays a critical role in carbon and nitrogen metabolism, but its structural information is unknown. Here we present the crystal structures of MoTps1 apo, binary (with UDPG) and ternary (with UDPG/G6P or UDP/T6P) complexes. MoTps1 consists of two modified Rossmann-fold domains and a catalytic center in-between. Unlike Escherichia coli OtsA (EcOtsA, the Tps1 of E. coli), MoTps1 exists as a mixture of monomer, dimer, and oligomer in solution. Inter-chain salt bridges, which are not fully conserved in EcOtsA, play primary roles in MoTps1 oligomerization. Binding of UDPG by MoTps1 C-terminal domain modifies the substrate pocket of MoTps1. In the MoTps1 ternary complex structure, UDP and T6P, the products of UDPG and G6P, are detected, and substantial conformational rearrangements of N-terminal domain, including structural reshuffling (beta3-beta4 loop to alpha0 helix) and movement of a 'shift region' towards the catalytic centre, are observed. These conformational changes render MoTps1 to a 'closed' state compared with its 'open' state in apo or UDPG complex structures. By solving the EcOtsA apo structure, we confirmed that similar ligand binding induced conformational changes also exist in EcOtsA, although no structural reshuffling involved. Based on our research and previous studies, we present a model for the catalytic process of Tps1. Our research provides novel information on MoTps1, Tps1 family, and structure-based antifungal drug design.

Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1.,Wang S, Zhao Y, Yi L, Shen M, Wang C, Zhang X, Yang J, Peng YL, Wang D, Liu J Biochem J. 2019 Nov 15;476(21):3227-3240. doi: 10.1042/BCJ20190289. PMID:31455720^[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
↑ Wang S, Zhao Y, Yi L, Shen M, Wang C, Zhang X, Yang J, Peng YL, Wang D, Liu J. Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1. Biochem J. 2019 Nov 15;476(21):3227-3240. doi: 10.1042/BCJ20190289. PMID:31455720 doi:http://dx.doi.org/10.1042/BCJ20190289

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6jak"

@@ Line 3: / Line 3: @@
 <StructureSection load='6jak' size='340' side='right'caption='[[6jak]], [[Resolution|resolution]] 2.41&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6jak]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JAK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JAK FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6jak]] is a 4 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=6JAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JAK FirstGlance]. <br>
-</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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.41&#8491;</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=6jak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jak OCA], [http://pdbe.org/6jak PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jak RCSB], [http://www.ebi.ac.uk/pdbsum/6jak PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jak 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=6jak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jak OCA], [https://pdbe.org/6jak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jak RCSB], [https://www.ebi.ac.uk/pdbsum/6jak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jak 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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Liu, J]]
+[[Category: Liu J]]
-[[Category: Wang, D]]
+[[Category: Wang D]]
-[[Category: Wang, S]]
+[[Category: Wang S]]
-[[Category: Zhao, Y]]
+[[Category: Zhao Y]]
-[[Category: Transferase]]
-[[Category: Trehalose-6-phosphate synthase]]

6jak

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OtsA apo structure

Structural highlights

Function

Publication Abstract from PubMed

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