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| [[Image:2fln.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_2fln| PDB=2fln | SCENE= }} | | {{STRUCTURE_2fln| PDB=2fln | SCENE= }} |
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| '''binary complex of catalytic core of human DNA polymerase iota with DNA (template A)'''
| | ===binary complex of catalytic core of human DNA polymerase iota with DNA (template A)=== |
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| ==Overview==
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| Substrate-induced conformational change of the protein is the linchpin of enzymatic reactions. Replicative DNA polymerases, for example, convert from an open to a closed conformation in response to dNTP binding. Human DNA polymerase-iota (hPoliota), a member of the Y family of DNA polymerases, differs strikingly from other polymerases in its much higher proficiency and fidelity for nucleotide incorporation opposite template purines than opposite template pyrimidines. We present here a crystallographic analysis of hPoliota binary complexes, which together with the ternary complexes show that, contrary to replicative DNA polymerases, the DNA, and not the polymerase, undergoes the primary substrate-induced conformational change. The incoming dNTP "pushes" templates A and G from the anti to the syn conformation dictated by a rigid hPoliota active site. Together, the structures posit a mechanism for template selection wherein dNTP binding induces a conformational switch in template purines for productive Hoogsteen base pairing.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16615915}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16615915 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16615915}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lesion bypass]] | | [[Category: Lesion bypass]] |
| [[Category: Template some]] | | [[Category: Template some]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:02:24 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:44:26 2008'' |
