View source for 3oh1


==Protein structure of USP from L. major bound to URIDINE-5'-DIPHOSPHATE-Galacturonic acid==
<StructureSection load='3oh1' size='340' side='right'caption='[[3oh1]], [[Resolution|resolution]] 2.18&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3oh1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OH1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OH1 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]] 2.18&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=UGB:(2S,3R,4S,5R,6R)-6-[[[(2R,3S,4R,5R)-5-(2,4-DIOXOPYRIMIDIN-1-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHOXY-HYDROXY-PHOSPHORYL]OXY-HYDROXY-PHOSPHORYL]OXY-3,4,5-TRIHYDROXY-OXANE-2-CARBOXYLIC+ACID'>UGB</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=3oh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oh1 OCA], [https://pdbe.org/3oh1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oh1 RCSB], [https://www.ebi.ac.uk/pdbsum/3oh1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oh1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D3G6S4_LEIMA D3G6S4_LEIMA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nucleotide sugars and the enzymes that are responsible for their synthesis are indispensable for the production of complex carbohydrates and, thus, for elaboration of a protective cellular coat for many organisms such as the protozoan parasite Leishmania. These activated sugars are synthesized de novo or derived from salvaged monosaccharides. In addition to UDP-glucose (UDP-Glc) pyrophosphorylase, which catalyzes the formation of UDP-Glc from substrates UTP and glucose-1-phosphate, Leishmania major and plants express a UDP-sugar pyrophosphorylase (USP) that exhibits broad substrate specificity in vitro. The enzyme, likely involved in monosaccharide salvage, preferentially generates UDP-Glc and UDP-galactose, but it may also activate other hexose- or pentose-1-phosphates such as galacturonic acid-1-phosphate or arabinose-1-phosphate. In order to gain insight into structural features governing the differences in substrate specificity, we determined the crystal structure of the L. major USP in the APO-, UTP-, and UDP-sugar-bound conformations. The overall tripartite structure of USP exhibits a significant structural homology to other nucleotidyldiphosphate-glucose pyrophosphorylases. The obtained USP structures reveal the structural rearrangements occurring during the stepwise binding process of the substrates. Moreover, the different product complexes explain the broad substrate specificity of USP, which is enabled by structural changes in the sugar binding region of the active site.

Structural Basis for the Broad Substrate Range of the UDP-Sugar Pyrophosphorylase from Leishmania major.,Dickmanns A, Damerow S, Neumann P, Schulz EC, Lamerz AC, Routier FH, Ficner R J Mol Biol. 2010 Nov 10. PMID:21073876<ref>PMID:21073876</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3oh1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leishmania major]]
[[Category: Damerow S]]
[[Category: Dickmanns A]]
[[Category: Ficner R]]
[[Category: Lamerz A]]
[[Category: Neumann P]]
[[Category: Routier F]]
[[Category: Schulz E-C]]