Abstract of the PDB Structure's related Publication:
Among RNA 5'-cap structures, γ-phosphate monomethylation is unique to a small subset of noncoding RNAs, 7SK and U6 in humans. 7SK is capped by methylphosphate capping enzyme (MePCE), which has a second nonenzymatic role as a core component of the 7SK ribonuclear protein (RNP), an essential regulator of RNA transcription. We report 2.0- and 2.1-Å X-ray crystal structures of the human MePCE methyltransferase domain bound to S-adenosylhomocysteine (SAH) and uncapped or capped 7SK substrates, respectively. 7SK recognition is achieved by protein contacts to a 5'-hairpin-single-stranded RNA region, thus explaining MePCE's specificity for 7SK and U6. The structures reveal SAH and product RNA in a near-transition-state geometry. Unexpectedly, binding experiments showed that MePCE has higher affinity for capped versus uncapped 7SK, and kinetic data support a model of slow product release. This work reveals the molecular mechanism of methyl transfer and 7SK retention by MePCE for subsequent assembly of 7SK RNP.
7SK snRNA methyl phosphate capping enzyme belongs to the S-adenosyl-L-methionine-dependent methyltransferase enzyme family (SMA). Specifically, BCDIN3 ads a methyl phosphate at the 5'-end of the 7SK snRNA (7SKRNA), stabilizing it (Xue et al. 2010 ; Jeronimo et al. 2007 ).
Noteworthy, it also has a non-enzymatic function as part of the 7SK RNP complex, sequestering the positive transcription elongation factor b(P-TEFb) in large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation nd subsequent transcriptional elongation (Xue et al. 2010 ; Jeronimo et al. 2007 ).