4MUM
Crystal structure of mitochondrial 5'(3')-deoxy ribonucleotidase alternative spliced variant
Summary for 4MUM
| Entry DOI | 10.2210/pdb4mum/pdb |
| Descriptor | Mitochondrial 5' nucleotidase, MAGNESIUM ION, PHOSPHATE ION, ... (9 entities in total) |
| Functional Keywords | 5'-nucleotidase, protein conformation, sequence homology, had-like, dephosphorylation, hydrolase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 25230.22 |
| Authors | Pachl, P.,Rezacova, P. (deposition date: 2013-09-22, release date: 2014-02-26, Last modification date: 2023-09-20) |
| Primary citation | Pachl, P.,Fabry, M.,Veverka, V.,Brynda, J.,Rezacova, P. Kinetic and structural characterization of an alternatively spliced variant of human mitochondrial 5'(3')-deoxyribonucleotidase. J Enzyme Inhib Med Chem, 30:63-68, 2015 Cited by PubMed Abstract: Human mitochondrial 5'(3')-deoxyribonucleotidase (mdN) catalyzes dephosphorylation of nucleoside monophosphates, and thus helps maintain homeostasis of deoxynucleosides required for mitochondrial DNA synthesis. Mature mdN is a 23-kDa dimeric protein with highest expression levels in the heart, brain and skeletal muscle. We have identified an alternative splice variant of the mdN gene containing an 18-nucleotide insertion encoding 6 amino acids (GKWPAT) at the 3'-end of the penultimate exon 4. We recombinantly expressed this enzyme variant and characterized its biochemical and kinetic properties as well as its three-dimensional structure. Our high-resolution (1.27 Å) crystal structure revealed that the insertion forms a loop located in the vicinity of the active site pocket and affects enzyme kinetic parameters as well as protein thermal stability. PubMed: 24506201DOI: 10.3109/14756366.2013.879577 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.271 Å) |
Structure validation
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