The three-dimensional structures of two isoforms of nucleoside diphosphate kinase from bovine retina
| Autor: | Najmoutin G. Abdulaev, Kevin D. Ridge, Maria Tordova, Gary L. Gilliland, Dmitri L. Kakuev, Jane E. Ladner |
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| Rok vydání: | 1999 |
| Předmět: |
Models
Molecular GTP' Protein Conformation Stereochemistry Trimer Random hexamer Crystallography X-Ray Retina Structural Biology Animals Humans Nucleotide chemistry.chemical_classification Binding Sites biology Nucleotides Kinase Active site General Medicine Nucleoside-diphosphate kinase Isoenzymes chemistry Biochemistry Nucleoside-Diphosphate Kinase Solvents biology.protein Cattle Nucleoside |
| Zdroj: | Acta Crystallographica Section D Biological Crystallography. 55:1127-1135 |
| ISSN: | 0907-4449 |
| DOI: | 10.1107/s0907444999002528 |
| Popis: | The crystal structures of two isoforms of nucleoside diphosphate kinase from bovine retina overexpressed in Escherischia coli have been determined to 2.4 Å resolution. Both the isoforms, NBR-A and NBR-B, are hexameric and the fold of the monomer is in agreement with NDP-kinase structures from other biological sources. Although the polypeptide chains of the two isoforms differ by only two residues, they crystallize in different space groups. NBR-A crystallizes in space group P212121 with an entire hexamer in the asymmetric unit, while NBR-B crystallizes in space group P43212 with a trimer in the asymmetric unit. The highly conserved nucleotide-binding site observed in other nucleoside diphosphate kinase structures is also observed here. Both NBR-A and NBR-B were crystallized in the presence of cGMP. The nucleotide is bound with the base in the anti conformation. The NBR-A active site contained both cGMP and GDP each bound at half occupancy. Presumably, NBR-A had retained GDP (or GTP) from the purification process. The NBR-B active site contained only cGMP. |
| Databáze: | OpenAIRE |
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