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| {{STRUCTURE_1leo| PDB=1leo | SCENE= }} | | {{STRUCTURE_1leo| PDB=1leo | SCENE= }} |
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| '''P100S NUCLEOSIDE DIPHOSPHATE KINASE'''
| | ===P100S NUCLEOSIDE DIPHOSPHATE KINASE=== |
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| ==Overview==
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| NDP kinase from Dictyostelium was mutated by site-directed mutagenesis at positions indicated by structural data to be involved in the trimer interface. The mutants were substitutions at residue Pro-100 (P100S and P100G) and deletions of 1-5 residues at the C terminus. Single mutants yielded proteins that kept both activity and hexameric structure. However, they were severely affected in their stability toward temperature and urea denaturation. When the P100S mutation was combined with any of the C-terminal deletions, the enzyme lost most of its activity and dissociated into dimers. Crystallographic analysis of the P100S protein was performed at 2.6 A resolution. The x-ray structure showed no direct alteration of intersubunits contacts at residue 100, but an induced disruption of the interaction between Asp-115 and the C terminus of another subunit. The substitution of proline 100 to serine corresponds to the Killer-of-prune mutation in Drosophila. Consequences of the mutation are discussed in view of the structural and biochemical properties observed in the mutant Dictyostelium protein.
| | The line below this paragraph, {{ABSTRACT_PUBMED_8702707}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 8702707 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_8702707}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Kinase]] | | [[Category: Kinase]] |
| [[Category: Transferase]] | | [[Category: Transferase]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:51:05 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:20:29 2008'' |
