View source for 6jbi


==Structure of Tps1 apo structure==
<StructureSection load='6jbi' size='340' side='right'caption='[[6jbi]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6jbi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyricularia_oryzae_70-15 Pyricularia oryzae 70-15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JBI 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]] 2.5&#8491;</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=6jbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jbi OCA], [https://pdbe.org/6jbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jbi RCSB], [https://www.ebi.ac.uk/pdbsum/6jbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jbi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G4NHF4_MAGO7 G4NHF4_MAGO7] 
<div style="background-color:#fffaf0;">
== 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<ref>PMID:31455720</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6jbi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pyricularia oryzae 70-15]]
[[Category: Liu J]]
[[Category: Wang D]]
[[Category: Wang S]]
[[Category: Yi L]]
[[Category: Zhao Y]]