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6BBO

Crystal structure of human APOBEC3H/RNA complex

Summary for 6BBO
Entry DOI10.2210/pdb6bbo/pdb
Related6B0B
DescriptorAPOBEC3H, RNA (5'-R(*UP*AP*AP*AP*AP*AP*AP*A)-3'), RNA (5'-R(*UP*UP*UP*UP*UP*UP*UP*U)-3'), ... (6 entities in total)
Functional Keywordsapobec, deaminase., hydrolase, hydrolase-rna complex, hydrolase/rna
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains8
Total formula weight102860.69
Authors
Shaban, N.M.,Shi, K.,Banerjee, S.,Harris, R.S.,Aihara, H. (deposition date: 2017-10-19, release date: 2018-01-10, Last modification date: 2024-10-30)
Primary citationShaban, N.M.,Shi, K.,Lauer, K.V.,Carpenter, M.A.,Richards, C.M.,Salamango, D.,Wang, J.,Lopresti, M.W.,Banerjee, S.,Levin-Klein, R.,Brown, W.L.,Aihara, H.,Harris, R.S.
The Antiviral and Cancer Genomic DNA Deaminase APOBEC3H Is Regulated by an RNA-Mediated Dimerization Mechanism.
Mol. Cell, 69:75-86.e9, 2018
Cited by
PubMed Abstract: Human APOBEC3H and homologous single-stranded DNA cytosine deaminases are unique to mammals. These DNA-editing enzymes function in innate immunity by restricting the replication of viruses and transposons. APOBEC3H also contributes to cancer mutagenesis. Here, we address the fundamental nature of RNA in regulating human APOBEC3H activities. APOBEC3H co-purifies with RNA as an inactive protein, and RNase A treatment enables strong DNA deaminase activity. RNA-binding-defective mutants demonstrate clear separation of function by becoming DNA hypermutators. Biochemical and crystallographic data demonstrate a mechanism in which double-stranded RNA mediates enzyme dimerization. Additionally, APOBEC3H separation-of-function mutants show that RNA binding is required for cytoplasmic localization, packaging into HIV-1 particles, and antiviral activity. Overall, these results support a model in which structured RNA negatively regulates the potentially harmful DNA deamination activity of APOBEC3H while, at the same time, positively regulating its antiviral activity.
PubMed: 29290613
DOI: 10.1016/j.molcel.2017.12.010
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.428 Å)
Structure validation

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