Crystal Structure of the Apicoplast DNA Polymerase from Plasmodium falciparum: The First Look at a Plastidic A-Family DNA Polymerase
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- 作者：Morgan E. Milton1 ; Jun-Yong Choe2 ; Richard B. Honzatko1 ; honzatko@iastate.edu" class="auth_mail" title="E-mail the corresponding author ; Scott W. Nelson1 ; swn@iastate.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：apPOL ; the polymerase domain encoded by the prex gene ; polymerase derived from Prex ; or apicoplast DNA polymerase ; Klenow ; the Klenow fragment of Escherichia coli DNA polymerase I ; BF ; the large fragment of the DNA polymerase from Geobacillus stearothermophilus ; T7 ; the DNA polymerase from bacteriophage T7 ; Taq ; the DNA polymerase from Thermus aquaticus ; polγ ; ; the DNA polymerase from human mitochondria ; N-apPOLexo ; &minus ; ; the D82N/E84Q mutant of apPOL with an N-terminal hexahis
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：9 October 2016
- 年：2016
- 卷：428
- 期：20
- 页码：3920-3934
- 全文大小：2071 K
文摘
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Replication of the apicoplast genome of Plasmodium falciparum sustains malaria infections.
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Apicoplast DNA polymerase (apPOL) is a bacterially derived atypical A-family polymerase.
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Divergent structural features of apPOL revealed here are probed by mutagenesis.
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Truncation of the novel N-terminal region eliminates apPOL proofreading activity.
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A known antimalarial compound is an in vitro inhibitor of apPOL.