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1rus

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[[Image:1rus.gif|left|200px]]
[[Image:1rus.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1rus |SIZE=350|CAPTION= <scene name='initialview01'>1rus</scene>, resolution 2.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1rus", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=3PG:3-PHOSPHOGLYCERIC+ACID'>3PG</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|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>
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1rus| PDB=1rus | SCENE= }}
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|RELATEDENTRY=
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|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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}}
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'''CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE'''
'''CRYSTAL STRUCTURE OF THE BINARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE AND ITS PRODUCT, 3-PHOSPHO-D-GLYCERATE'''
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[[Category: Lundqvist, T.]]
[[Category: Lundqvist, T.]]
[[Category: Schneider, G.]]
[[Category: Schneider, G.]]
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[[Category: lyase(carbon-carbon)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:56:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:33:14 2008''
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Revision as of 04:56, 3 May 2008

Image:1rus.gif

Template:STRUCTURE 1rus

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 Page seeded by OCA on Sat May 3 07:56:14 2008

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