2rus: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
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

File: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 "https://proteopedia.org/index.php?title=2rus&oldid=660035"