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Structure of the catalytic chain of Methanococcus jannaschii aspartate transcarbamoylase in a hexagonal crystal form: Insights into the path of carbamoyl phosphate to the active site of the enzyme

Journal Article · · Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Crystals of the catalytic chain of Methanococcus jannaschii aspartate transcarbamoylase (ATCase) grew in the presence of the regulatory chain in the hexagonal space group P6{sub 3}22, with one monomer per asymmetric unit. This is the first time that crystals with only one monomer in the asymmetric unit have been obtained; all known structures of the catalytic subunit contain several crystallographically independent monomers. The symmetry-related chains form the staggered dimer of trimers observed in the other known structures of the catalytic subunit. The central channel of the catalytic subunit contains a sulfate ion and a K{sup +} ion as well as a glycerol molecule at its entrance. It is possible that it is involved in channeling carbamoyl phosphate (CP) to the active site of the enzyme. A second sulfate ion near Arg164 is near the second CP position in the wild-type Escherichia coli ATCase structure complexed with CP. It is suggested that this position may also be in the path that CP takes when binding to the active site in a partial diffusion process at 310 K. Additional biochemical studies of carbamoylation and the molecular organization of this enzyme in M. jannaschii will provide further insight into these points.
Research Organization:
BROOKHAVEN NATIONAL LABORATORY (BNL)
Sponsoring Organization:
USDOE SC OFFICE OF BIOLOGICAL & ENVIRONMENTAL RESEARCH
DOE Contract Number:
AC02-98CH10886
OSTI ID:
1046994
Report Number(s):
BNL--98107-2012-JA; KP1605010
Journal Information:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Journal Name: Acta Crystallographica Section F: Structural Biology and Crystallization Communications Journal Issue: 5 Vol. 68; ISSN 1744-3091
Country of Publication:
United States
Language:
English

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