3oh4 | pdb_00003oh4

Protein structure of USP from L. major bound to URIDINE-5'-DIPHOSPHATE Glucose

spinqualitylabelsall models 3oh4, resolution 2.21Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3oh4 is a 1 chain structure with sequence from Leima. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL, UPG Related: 3oh0, 3oh1, 3oh2, 3oh3, 3ogz Gene: USP (LEIMA) Activity: UTP-monosaccharide-1-phosphate uridylyltransferase, with EC number 2.7.7.64 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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