A polymerase I palm in adenylyl cyclase?
| Autor: | Peter Willett, Peter J. Artymiuk, David W. Rice, Andrew R. Poirrette |
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| Rok vydání: | 1997 |
| Předmět: |
Models
Molecular Protein Folding Gs alpha subunit Protein Conformation Molecular Sequence Data ADCY10 Catalysis Adenylyl cyclase Evolution Molecular chemistry.chemical_compound Structure-Activity Relationship Adenosine Triphosphate Polymerase Multidisciplinary Binding Sites Thermus aquaticus biology ADCY9 biology.organism_classification DNA Polymerase I chemistry Biochemistry biology.protein cAMP-dependent pathway DNA polymerase I Adenylyl Cyclases |
| Zdroj: | Nature. 388(6637) |
| ISSN: | 0028-0836 |
| Popis: | Zhang et al.1 recently reported the long-awaited structure determination of one of the catalytic core domains of eukaryotic adenylyl cyclase, which promises a greater understanding of the regulatory mechanisms associated with the use of cyclic AMP as a second messenger. We have searched the Brookhaven Protein Data Bank2 using the program PROTEP3 and found that, far from having a completely novel fold, the fold of the domain bears an extraordinary resemblance to the ‘palm’ domains of the polymerase I family of prokaryotic DNA polymerases, including Escherichia coli DNA polymerase I4,5 and Thermus aquaticus ( Taq) polymerase6,7. The similarity has important implications for the function and evolution of eukaryotic adenylyl cyclases and related proteins. |
| Databáze: | OpenAIRE |
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