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| - | [[Image:1ncl.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1ncl| PDB=1ncl | SCENE= }} | | {{STRUCTURE_1ncl| PDB=1ncl | SCENE= }} |
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| - | '''THERMAL STABILITY OF HEXAMERIC AND TETRAMERIC NUCLEOSIDE, DIPHOSPHATE KINASES'''
| + | ===THERMAL STABILITY OF HEXAMERIC AND TETRAMERIC NUCLEOSIDE, DIPHOSPHATE KINASES=== |
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| - | ==Overview==
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| - | The eukaryotic nucleoside diphosphate (NDP) kinases are hexamers, while the bacterial NDP kinases are tetramers made of small, single domain subunits. These enzymes represent an ideal model for studying the effect of subunit interaction on protein stability. The thermostability of NDP kinases of each class was studied by differential scanning calorimetry and biochemical methods. The hexameric NDP kinase from Dictyostelium discoideum displays one single, irreversible differential scanning calorimetry peak (Tm 62 degrees C) over a broad protein concentration, indicating a single step denaturation. The thermal stability of the protein was increased by ADP. The P105G substitution, which affects a loop implicated in subunit contacts, yields a protein that reversibly dissociates to folded monomers at 38 degrees C before the irreversible denaturation occurs (Tm 47 degrees C). ADP delays the dissociation, but does not change the Tm. These data indicate a "coupling" of the quaternary structure with the tertiary structure in the wild-type, but not in the mutated protein. We describe the x-ray structure of the P105G mutant at 2.2-A resolution. It is very similar to that of the wild-type protein. Therefore, a minimal change in the structure leads to a dramatic change of protein thermostability. The NDP kinase from Escherichia coli behaves like the P105G mutant of the Dictyostelium NDP kinase. The detailed study of their thermostability is important, since biological effects of thermolabile NDP kinases have been described in several organisms. | + | The line below this paragraph, {{ABSTRACT_PUBMED_8663370}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8663370 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8663370}} |
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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 Sat May 3 02:22:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:48:53 2008'' |
Revision as of 14:48, 28 July 2008
Template:STRUCTURE 1ncl
THERMAL STABILITY OF HEXAMERIC AND TETRAMERIC NUCLEOSIDE, DIPHOSPHATE KINASES
Template:ABSTRACT PUBMED 8663370
About this Structure
1NCL is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
Thermal stability of hexameric and tetrameric nucleoside diphosphate kinases. Effect of subunit interaction., Giartosio A, Erent M, Cervoni L, Morera S, Janin J, Konrad M, Lascu I, J Biol Chem. 1996 Jul 26;271(30):17845-51. PMID:8663370
Page seeded by OCA on Mon Jul 28 17:48:53 2008
