3ukh | pdb_00003ukh

Crystal structure of udp-galactopyranose mutase from Aspergillus fumigatus in complex with UDPGALP (non-reduced)

spinqualitylabelsall models 3ukh, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ukh is a 8 chain structure with sequence from Aspergillus fumigatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, FAD, FDA, GDU Related: 3uka, 3ukf, 3ukk, 3ukl, 3ukp, 3ukq Gene: glf, glfA (Aspergillus fumigatus) Activity: UDP-galactopyranose mutase, with EC number 5.4.99.9 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed UDP-galactopyranose mutase (UGM) is a flavin-containing enzyme that catalyzes the reversible conversion of UDP-galactopyranose (UDP-Galp) to UDP-galactofuranose (UDP-Galf). As in prokaryotic UGMs, the flavin needs to be reduced for the enzyme to be active. Here we present the first eukaryotic UGM structures from Aspergillus fumigatus (AfUGM). The structures are of UGM alone, with the substrate UDP-Galp and with the inhibitor UDP. Additionally, we report the structures of AfUGM bound to substrate with oxidized and educed flavin. These structures provide insight into substrate recognition and structural changes observed upon substrate binding involving the mobile loops and the critical arginine residues R182 and R327. Comparison with prokaryotic UGM reveals that despite low sequence identity with known prokaryotic UGMs the overall fold is largely conserved. Structural differences between prokaryotic UGM and AfUGM result from inserts in AfUGM. A notable difference from prokaryotic UGMs is that AfUGM contains a third flexible loop (loop III) above the si-face of the isoalloxazine ring that changes position depending on the redox state of the flavin cofactor. This loop flipping has not been observed in prokaryotic UGMs. In addition we have determined the crystals structures and steady-state kinetic constants of the reaction catalyzed by mutants R182K, R327K, R182A and R327A. These results support our hypothesis that R182 and R327 play important roles in stabilizing the diphosphates of the nucleotide sugar and help to facilitate the positioning of the galactose moiety for catalysis. Structural insight into the unique substrate binding mechanism and flavin redox state of UDP-galactopyranose mutase from Aspergillus fumigatus.,van Straaten KE, Routier FH, Sanders DA J Biol Chem. 2012 Feb 10. PMID:22334662 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also UDP-galactopyranose mutase

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