Molecular Playground/DNA replication initiator DnaA: Difference between revisions
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DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state. | DnaA function is regulated by different nucleotide binding state. In ATP bound state, DnaA can recognize more binding elements on the chromosome(called DnaA box), and initiate replication by unwinding specific region in the DNA and recruit DnaB helicase. However, after the ATP hydrolysis, DnaA-ADP becomes an inactive protein. This activity change was shown to be associated with its oligomeric assembly state. | ||
=== DnaA Monomer Structure === | === DnaA Monomer Structure === | ||
The <scene name='User:Jing_Liu/Sandbox_1/1/4'>structure of DnaA</scene> in ''Aquifex aeolicus'' was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the <scene name='User:Jing_Liu/Sandbox_1/2/1'>complex</scene> in ''Mycobacterium tuberculosis''[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. | The <scene name='User:Jing_Liu/Sandbox_1/1/4'>structure of DnaA</scene> in ''Aquifex aeolicus'' was solved in 2002[http://www.ncbi.nlm.nih.gov/pubmed/12234917?dopt=Abstract], and it contains the linker region, AAA+ domain and DNA binding domain(DBD). The interaction with DNA is through the recognization of a conserved 9 bp DNA recognition sequence (TTA/TTNCACC), and this was shown by the crystal structure of the <scene name='User:Jing_Liu/Sandbox_1/2/1'>complex</scene> in ''Mycobacterium tuberculosis''[http://www.ncbi.nlm.nih.gov/pubmed/21620858?dopt=Abstract]. | ||
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<Structure load='1L8Q' size='300' frame='true' align='right' caption='2HCB tetramer' scene='User:Jing_Liu/Sandbox_1/3/3' /> | <Structure load='1L8Q' size='300' frame='true' align='right' caption='2HCB tetramer' scene='User:Jing_Liu/Sandbox_1/3/3' /> | ||
The crystal structure of AMP-PCP-bound DnaA reveals a <scene name='User:Jing_Liu/Sandbox_1/3/3'>right-handed superhelix</scene> structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230. | The crystal structure of AMP-PCP-bound DnaA reveals a <scene name='User:Jing_Liu/Sandbox_1/3/3'>right-handed superhelix</scene> structure[http://www.ncbi.nlm.nih.gov/pubmed/16829961?dopt=Abstract]. Each monomer contact with another two monomers to form a filamentous structure. The engagement of ATP involved the arginine figure at position 230. | ||
=== 3D structures of DnaA === | |||
See [[DnaA]] | |||
=== Reference === | === Reference === |