4nd4

Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (pyruvic acid) and cofactor (b-nicotinamide adenine dinucleotide)Crystal structure of the lactate dehydrogenase from cryptosporidium parvum complexed with substrate (pyruvic acid) and cofactor (b-nicotinamide adenine dinucleotide)

Structural highlights 4nd4 is a 2 chain structure with sequence from Cryptosporidium parvum Iowa II. This structure supersedes the now removed PDB entry 2fm3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5CYZ2_CRYPI Publication Abstract from PubMed The protozoan parasite Cryptosporidium parvum causes waterborne diseases worldwide. There is no effective therapy for C. parvum infection. The parasite depends mainly on glycolysis for energy production. Lactate dehydrogenase is a major regulator of glycolysis. This paper describes the biochemical characterization of C. parvum lactate dehydrogenase and high resolution crystal structures of the apo-enzyme and four ternary complexes. The ternary complexes capture the enzyme bound to NAD/NADH or its 3-acetylpyridine analog in the cofactor binding pocket, while the substrate binding site is occupied by one of the following ligands: lactate, pyruvate or oxamate. The results reveal distinctive features of the parasitic enzyme. For example, C. parvum lactate dehydrogenase prefers the acetylpyridine analog of NADH as a cofactor. Moreover, it is slightly less sensitive to gossypol inhibition compared with mammalian lactate dehydrogenases and not inhibited by excess pyruvate. The active site loop and the antigenic loop in C. parvum lactate dehydrogenase are considerably different from those in the human counterpart. Structural features and enzymatic properties of C. parvum lactate dehydrogenase are similar to enzymes from related parasites. Structural comparison with malate dehydrogenase supports a common ancestry for the two genes. Biochemical and structural characterization of Cryptosporidium parvum Lactate dehydrogenase.,Cook WJ, Senkovich O, Hernandez A, Speed H, Chattopadhyay D Int J Biol Macromol. 2015 Mar;74:608-19. doi: 10.1016/j.ijbiomac.2014.12.019., Epub 2014 Dec 24. PMID:25542170 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Lactate Dehydrogenase Lactate dehydrogenase 3D structures

spinqualitylabelsall models 4nd4, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image