1rba

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rba.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1rba.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rba| PDB=1rba | SCENE= }}
{{STRUCTURE_1rba| PDB=1rba | SCENE= }}
-
'''SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES'''
+
===SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES===
-
==Overview==
+
<!--
-
The crystal structure of a mutant of ribulose bisphosphate carboxylase/oxygenase from Rhodospirillium rubrum, where Asp193, one of the ligands of the magnesium ion at the activator site, is replaced by Asn, has been determined to a nominal resolution of 0.26 nm. The mutation of Asp to Asn induces both local and global conformation changes as follows. The side chain of Asn193 moves away from the active site and interacts with main-chain oxygen of residue 165, located in the neighbouring strand beta 1 of the alpha/beta barrel. The side chain of Lys166, which forms a salt bridge with Asp193 in the wild-type enzyme, interacts with Asn54 from the second subunit and creates a new subunit-subunit interaction. Another new subunit-subunit interaction is formed, more than 1.2 nm away from the site of the mutation. In the mutant enzyme, the side chain of Asp263 interacts with the side chain of Thr106 from the second subunit. Asp193 is not part of a subunit-subunit interface area or an allosteric regulatory site. Nevertheless, replacement of this residue by Asn results, unexpectedly, in a difference in the packing of the two subunits, which can be described as a slight rotation of one of the subunits relative to the second. The observed structural changes at the active site of the enzyme provide a molecular explanation for the differing behaviour of the Asp193----Asn mutant with respect to activation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_1606957}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 1606957 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_1606957}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Schneider, G.]]
[[Category: Schneider, G.]]
[[Category: Soderlind, E.]]
[[Category: Soderlind, E.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:17:51 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:19:02 2008''

Revision as of 03:19, 29 July 2008

Image:1rba.png

Template:STRUCTURE 1rba

SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES

Template:ABSTRACT PUBMED 1606957

About this Structure

1RBA is a Single protein structure of sequence from Rhodospirillum rubrum. Full crystallographic information is available from OCA.

Reference

Substitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes., Soderlind E, Schneider G, Gutteridge S, Eur J Biochem. 1992 Jun 15;206(3):729-35. PMID:1606957

Page seeded by OCA on Tue Jul 29 06:19:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rba"
Personal tools