1aus
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(New page: 200px<br /><applet load="1aus" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aus, resolution 2.2Å" /> '''ACTIVATED UNLIGANDED ...)
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Revision as of 09:01, 20 November 2007
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ACTIVATED UNLIGANDED SPINACH RUBISCO
Overview
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, solution. The present structure points to direct participation of the, active site side chain of lysine 175 in later stages of catalysis. This, possibility is discussed in the light of mutagenesis studies.
About this Structure
1AUS is a Protein complex structure of sequences from Spinacia oleracea with MG and FMT as ligands. Active as Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 Full crystallographic information is available from OCA.
Reference
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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