Abstract:
:The crystal structure of the N-terminal domain of the RNA polymerase δ subunit (Nδ) from Bacillus subtilis solved at a resolution of 2.0Å is compared with the NMR structure determined previously. The molecule crystallizes in the space group C222(1) with a dimer in the asymmetric unit. Importantly, the X-ray structure exhibits significant differences from the lowest energy NMR structure. In addition to the overall structure differences, structurally important β sheets found in the NMR structure are not present in the crystal structure. We systematically investigated the cause of the discrepancies between the NMR and X-ray structures of Nδ, addressing the pH dependence, presence of metal ions, and crystal packing forces. We convincingly showed that the crystal packing forces, together with the presence of Ni(2+) ions, are the main reason for such a difference. In summary, the study illustrates that the two structural approaches may give unequal results, which need to be interpreted with care to obtain reliable structural information in terms of biological relevance.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Demo G,Papoušková V,Komárek J,Kadeřávek P,Otrusinová O,Srb P,Rabatinová A,Krásný L,Žídek L,Sklenář V,Wimmerová Mdoi
10.1016/j.jsb.2014.06.001subject
Has Abstractpub_date
2014-08-01 00:00:00pages
174-186issue
2eissn
1047-8477issn
1095-8657pii
S1047-8477(14)00137-3journal_volume
187pub_type
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