1upm
From Proteopedia
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ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-CARBOXYARABINITOL 2 BISPHOSPHAT AND CA2+.
Overview
Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase) catalyses CO(2), assimilation in biology. A prerequisite for catalysis is an activation, process, whereby an active site lysine is selectively carbamylated. The, carbamyl group is then stablised by a metal ion, which in vivo is Mg(2+)., Other divalent metal ions can replace Mg(2+) as activators in vitro, but, the nature of the metal ion strongly influences the catalytic activity of, the enzyme and has a differential effect on the ratio of the carboxylation, reaction and the competing oxygenation reaction. Biochemical studies show, that calcium promotes carbamylation but not catalysis. To investigate the, role of the metal in catalysis, we have determined two structures of the, enzyme complexed with Ca(2+) and the transition state ... [(full description)]
About this Structure
1UPM is a [Protein complex] structure of sequences from [Spinacia oleracea] with CA and CAP as [ligands]. Active as [Ribulose-bisphosphate carboxylase], with EC number [4.1.1.39]. Structure known Active Site: ACL. Full crystallographic information is available from [OCA].
Reference
Calcium supports loop closure but not catalysis in Rubisco., Karkehabadi S, Taylor TC, Andersson I, J Mol Biol. 2003 Nov 14;334(1):65-73. PMID:14596800
Page seeded by OCA on Tue Oct 30 16:08:05 2007
