3KO8
Crystal Structure of UDP-galactose 4-epimerase
Summary for 3KO8
| Entry DOI | 10.2210/pdb3ko8/pdb |
| Descriptor | NAD-dependent epimerase/dehydratase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | isomerase, udp-galactose 4-epimerase |
| Biological source | Pyrobaculum calidifontis |
| Total number of polymer chains | 1 |
| Total formula weight | 35154.92 |
| Authors | Sakuraba, H.,Kawai, T.,Yoneda, K.,Ohshima, T. (deposition date: 2009-11-13, release date: 2010-11-17, Last modification date: 2023-11-01) |
| Primary citation | Sakuraba, H.,Kawai, T.,Yoneda, K.,Ohshima, T. Crystal structure of UDP-galactose 4-epimerase from the hyperthermophilic archaeon Pyrobaculum calidifontis Arch.Biochem.Biophys., 512:126-134, 2011 Cited by PubMed Abstract: The crystal structure of a highly thermostable UDP-galactose 4-epimerase (GalE) from the hyperthermophilic archaeon Pyrobaculum calidifontis was determined at a resolution of 1.8Å. The asymmetric unit contained one subunit, and the functional dimer was generated by a crystallographic two-fold axis. Each monomer consisted of a Rossmann-fold domain with NAD bound and a carboxyl terminal domain. The overall structure of P. calidifontis GalE showed significant similarity to the structures of the GalEs from Escherichia coli, human and Trypanosoma brucei. However, the sizes of several surface loops were markedly smaller in P. calidifontis GalE than the corresponding loops in the other enzymes. Structural comparison revealed that the presence of an extensive hydrophobic interaction at the subunit interface is likely the main factor contributing to the hyperthermostability of the P. calidifontis enzyme. Within the NAD-binding site of P. calidifontis GalE, a loop (NAD-binding loop) tightly holds the adenine ribose moiety of NAD. Moreover, a deletion mutant lacking this loop bound NAD in a loose, reversible manner. Thus the presence of the NAD-binding loop in GalE is largely responsible for preventing the release of the cofactor from the holoenzyme. PubMed: 21645492DOI: 10.1016/j.abb.2011.05.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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