A PII-Like Protein Regulated by Bicarbonate: Structural and Biochemical Studies of the Carboxysome-Associated CPII Protein
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- 作者：Nicole M. Wheatley1 ; Kevin D. Eden2 ; Joanna Ngo2 ; Justin S. Rosinski2 ; Michael R. Sawaya1 ; Duilio Cascio1 ; Michael Collazo1 ; Hamidreza Hoveida2 ; Wayne L. Hubbell2 ; 3 ; Todd O. Yeates1 ; 2 ; yeates@mbi.ucla.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：RuBisCO ; ribulose-1 ; 5-bisphosphate carboxylase/oxygenase ; CCM ; carbon concentrating mechanisms ; nrPII ; nitrogen regulatory PII protein ; NDH-5 ; NADH&ndash ; ubiquinone oxidoreductase chain 5 homolog ; PDB ; Protein Data Bank ; CPII ; carboxysome-associated PII protein ; EPR ; electron paramagnetic resonance
- 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：4013-4030
- 全文大小：3648 K
文摘
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A protein related to nitrogen PII proteins is conserved near α-carboxysome genes.
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Crystal structures of CPII are elucidated with and without potential ligands.
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ADP and AMP binding drive major conformational changes in the protein trimer.
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Bicarbonate, a substrate of carboxysomes, enhances ADP and AMP binding.
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A unique clade of PII proteins, herein named CPII, is regulated by inorganic carbon.