Abstract:
:The prokaryotic tubulin homologue FtsZ polymerizes in vitro in a nucleotide dependent fashion. Here we report that replacement of the strictly conserved Asp212 residue of Escherichia coli FtsZ by a Cys or Asn, but not by a Glu residue results in FtsZ that polymerizes with divalent cations in the absence of added GTP. FtsZ D212C and D212N mutants co-purify with GTP as bound nucleotide, providing an explanation for the unusual phenotype. We conclude that D212 plays a critical role in the coordination of a metal ion and the nucleotide at the interface of two FtsZ monomers.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Scheffers DJ,de Wit JG,den Blaauwen T,Driessen AJdoi
10.1016/s0014-5793(01)02310-9keywords:
subject
Has Abstractpub_date
2001-04-06 00:00:00pages
34-7issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02310-9journal_volume
494pub_type
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