1aa1
From Proteopedia
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|PDB= 1aa1 |SIZE=350|CAPTION= <scene name='initialview01'>1aa1</scene>, resolution 2.2Å | |PDB= 1aa1 |SIZE=350|CAPTION= <scene name='initialview01'>1aa1</scene>, resolution 2.2Å | ||
|SITE= <scene name='pdbsite=ACB:Active+Site'>ACB</scene>, <scene name='pdbsite=ACE:Active+Site'>ACE</scene>, <scene name='pdbsite=ACH:Active+Site'>ACH</scene> and <scene name='pdbsite=ACL:Active+Site'>ACL</scene> | |SITE= <scene name='pdbsite=ACB:Active+Site'>ACB</scene>, <scene name='pdbsite=ACE:Active+Site'>ACE</scene>, <scene name='pdbsite=ACH:Active+Site'>ACH</scene> and <scene name='pdbsite=ACL:Active+Site'>ACL</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aa1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aa1 OCA], [http://www.ebi.ac.uk/pdbsum/1aa1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aa1 RCSB]</span> | ||
}} | }} | ||
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[[Category: Andersson, I.]] | [[Category: Andersson, I.]] | ||
[[Category: Taylor, T C.]] | [[Category: Taylor, T C.]] | ||
| - | [[Category: 3PG]] | ||
| - | [[Category: MG]] | ||
[[Category: lyase (carbon-carbon)]] | [[Category: lyase (carbon-carbon)]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:36:23 2008'' |
Revision as of 15:36, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , and | ||||||
| Ligands: | , , | ||||||
| Activity: | Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ACTIVATED SPINACH RUBISCO IN COMPLEX WITH THE PRODUCT 3-PHOSPHOGLYCERATE
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
1AA1 is a Protein complex structure of sequences from Spinacia oleracea. 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
Page seeded by OCA on Sun Mar 30 18:36:23 2008
