2rus

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[[Image:2rus.jpg|left|200px]]<br /><applet load="2rus" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2rus.jpg|left|200px]]
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caption="2rus, resolution 2.3&Aring;" />
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'''CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE, MG(II), AND ACTIVATOR CO2 AT 2.3-ANGSTROMS RESOLUTION'''<br />
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{{Structure
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|PDB= 2rus |SIZE=350|CAPTION= <scene name='initialview01'>2rus</scene>, resolution 2.3&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=FOR:FORMYL GROUP'>FOR</scene>
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|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]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE, MG(II), AND ACTIVATOR CO2 AT 2.3-ANGSTROMS RESOLUTION'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2RUS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=FOR:'>FOR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUS OCA].
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2RUS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RUS OCA].
==Reference==
==Reference==
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Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution., Lundqvist T, Schneider G, Biochemistry. 1991 Jan 29;30(4):904-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1899197 1899197]
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Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution., Lundqvist T, Schneider G, Biochemistry. 1991 Jan 29;30(4):904-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1899197 1899197]
[[Category: Rhodospirillum rubrum]]
[[Category: Rhodospirillum rubrum]]
[[Category: Ribulose-bisphosphate carboxylase]]
[[Category: Ribulose-bisphosphate carboxylase]]
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[[Category: lyase(carbon-carbon)]]
[[Category: lyase(carbon-carbon)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:48:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:38:09 2008''

Revision as of 16:38, 20 March 2008


PDB ID 2rus

Drag the structure with the mouse to rotate
, resolution 2.3Å
Ligands: and
Activity: Ribulose-bisphosphate carboxylase, with EC number 4.1.1.39
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE, MG(II), AND ACTIVATOR CO2 AT 2.3-ANGSTROMS RESOLUTION


Overview

The activated ternary complex, enzyme-CO2-Mg(II), of the dimeric ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum can be prepared in the same crystal form that was used for the crystallographic structure determination of the native nonactivated enzyme (Schneider, G., Branden, C.-I., & Lorimer, G. (1986) J. Mol. Biol. 187, 141-143). The three-dimensional structure of the activated enzyme has been determined to a nominal resolution of 2.3 A by protein crystallographic methods. The activator CO2 forms a carbamate with Lys191, located at the bottom of the funnel-shaped active site. In both subunits, this labile adduct is stabilized by a Mg(II) ion, bound to the carbamate and the side chains of Asp193 and Glu194. One solvent molecule was found within the first coordination sphere of the metal ion. The metal-binding site in ribulose-1,5-bisphosphate carboxylase consists thus of at least three protein ligands, all located on loop 2 of the beta/alpha barrel. One additional metal ligand, the side chain of the conserved Asn111, was observed close to the Mg(II) ion in the B-subunit. Other structural differences at the active site between the activated and nonactivated enzyme are limited to side-chain positions. Nevertheless, it is obvious that the hydrogen-bonding pattern in the vicinity of the activator site is completely altered.

About this Structure

2RUS is a Single protein structure of sequence from Rhodospirillum rubrum. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ternary complex of ribulose-1,5-bisphosphate carboxylase, Mg(II), and activator CO2 at 2.3-A resolution., Lundqvist T, Schneider G, Biochemistry. 1991 Jan 29;30(4):904-8. PMID:1899197

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