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1rus
From Proteopedia
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|PDB= 1rus |SIZE=350|CAPTION= <scene name='initialview01'>1rus</scene>, resolution 2.9Å | |PDB= 1rus |SIZE=350|CAPTION= <scene name='initialview01'>1rus</scene>, resolution 2.9Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC ACID'>3PG</scene> | + | |LIGAND= <scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</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=1rus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rus OCA], [http://www.ebi.ac.uk/pdbsum/1rus PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rus RCSB]</span> | ||
}} | }} | ||
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[[Category: Lundqvist, T.]] | [[Category: Lundqvist, T.]] | ||
[[Category: Schneider, G.]] | [[Category: Schneider, G.]] | ||
| - | [[Category: 3PG]] | ||
[[Category: lyase(carbon-carbon)]] | [[Category: lyase(carbon-carbon)]] | ||
| - | ''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 23:33:14 2008'' |
Revision as of 20:33, 30 March 2008
| |||||||
| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE
Overview
The crystal structure of the binary complex of non-activated ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum and its product 3-phospho-D-glycerate has been determined to 2.9-A resolution. This structure determination confirms the proposed location of the active site (Schneider, G., Lindqvist, Y., Branden, C.-I., and Lorimer, G. (1986) EMBO J. 5, 3409-3415) at the carboxyl end of the beta-strands of the alpha/beta-barrel in the carboxyl-terminal domain. One molecule of 3-phosphoglycerate is bound per active site. All oxygen atoms of 3-phosphoglycerate form hydrogen bonds to groups of the enzyme. The phosphate group interacts with the sidechains of residues Arg-288, His-321, and Ser-368, which are conserved between enzymes from different species as well as with the main chain nitrogens from residues Thr-322 and Gly-323. These amino acid residues constitute one of the two phosphate binding sites of the active site. The carboxyl group interacts with the side chains of His-287, Lys-191, and Asn-111. Implications of the activation process for the binding of 3-phosphoglycerate are discussed.
About this Structure
1RUS is a Single protein structure of sequence from Rhodospirillum rubrum. Full crystallographic information is available from OCA.
Reference
Crystal structure of the binary complex of ribulose-1,5-bisphosphate carboxylase and its product, 3-phospho-D-glycerate., Lundqvist T, Schneider G, J Biol Chem. 1989 Mar 5;264(7):3643-6. PMID:2492987
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