4nd3 | pdb_00004nd3

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

spinqualitylabelsall models 4nd3, resolution 2.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nd3 is a 2 chain structure with sequence from Crypi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 2OP, GOL, NAD Related: 4nd1, 4nd2, 4nd4, 4nd5 Gene: cgd7_480, LDH1 (CRYPI) Activity: L-lactate dehydrogenase, with EC number 1.1.1.27 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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.

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