1aus: Difference between revisions
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[[Image:1aus.gif|left|200px]] | [[Image:1aus.gif|left|200px]] | ||
'''ACTIVATED UNLIGANDED SPINACH RUBISCO''' | {{Structure | ||
|PDB= 1aus |SIZE=350|CAPTION= <scene name='initialview01'>1aus</scene>, resolution 2.2Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Ribulose-bisphosphate_carboxylase Ribulose-bisphosphate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.39 4.1.1.39] | |||
|GENE= | |||
}} | |||
'''ACTIVATED UNLIGANDED SPINACH RUBISCO''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AUS is a [ | 1AUS is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUS OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9092835 9092835] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ribulose-bisphosphate carboxylase]] | [[Category: Ribulose-bisphosphate carboxylase]] | ||
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[[Category: lyase (carbon-carbon)]] | [[Category: lyase (carbon-carbon)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:32 2008'' |
Revision as of 11:02, 20 March 2008
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, resolution 2.2Å | |||||||
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Ligands: | and | ||||||
Activity: | Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
ACTIVATED UNLIGANDED SPINACH RUBISCO
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 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 StructureAbout this Structure
1AUS is a Protein complex structure of sequences from Spinacia oleracea. 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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