1aa1

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File:1aa1.gif


1aa1, resolution 2.2Å

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ACTIVATED SPINACH RUBISCO IN COMPLEX WITH THE PRODUCT 3-PHOSPHOGLYCERATE

OverviewOverview

The crystal structure of an activated complex of ribulose-1,5-bisphosphate, carboxylase/oxygenase from spinach and its product 3-phosphoglycerate has, been determined to 2.2 A resolution. The structure is of the open form, with the active site accessible to the solvent as observed in the, structures of the activated ligand-free enzyme and the complex of the, activated enzyme with the substrate ribulose-1,5-bisphosphate. Two, molecules of 3-phosphoglycerate are bound per active site. The phosphates, of both molecules bind approximately at the same position as the, phosphates of ribulose-1,5-bisphosphate or the six-carbon intermediate, analogue 2-carboxyarabinitol-1,5-bisphosphate, but one product molecule is, swung out from the active site with its carboxylate group pointing toward, ... [(full description)]

About this StructureAbout this Structure

1AA1 is a [Protein complex] structure of sequences from [Spinacia oleracea] with MG and 3PG as [ligands]. Active as [Ribulose-bisphosphate carboxylase], with EC number [4.1.1.39]. Structure known Active Sites: ACB, ACE, ACH and ACL. Full crystallographic information is available from [OCA].

ReferenceReference

Structure of a product complex of spinach ribulose-1,5-bisphosphate carboxylase/oxygenase., Taylor TC, Andersson I, Biochemistry. 1997 Apr 1;36(13):4041-6. PMID:9092835

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