This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2rus

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2rus.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2rus.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2rus| PDB=2rus | SCENE= }}
{{STRUCTURE_2rus| PDB=2rus | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE, MG(II), AND ACTIVATOR CO2 AT 2.3-ANGSTROMS RESOLUTION'''
+
===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., &amp; 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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1899197}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1899197 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1899197}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Lundqvist, T.]]
[[Category: Lundqvist, T.]]
[[Category: Schneider, G.]]
[[Category: Schneider, G.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 17:16:59 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:13:03 2008''

Revision as of 15:13, 27 July 2008

Image:2rus.png

Template:STRUCTURE 2rus

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

Template:ABSTRACT PUBMED 1899197

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

Page seeded by OCA on Sun Jul 27 18:13:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2rus"
Personal tools