1gn2: Difference between revisions

Line 1:

[[Image:1gn2.~~jpg~~|left|200px]]

[[Image:1gn2.png|left|200px]]

<!--

Line 9:

Line 10:

~~'''~~S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.~~'''~~

===S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.===

~~==Overview==~~

<!--

~~With the aim of enhancing interactions involved in dimer formation~~, ~~an intersubunit disulfide bridge was engineered in~~ the ~~superoxide dismutase enzyme of Mycobacterium tuberculosis. Ser-123 was chosen for mutation~~ to ~~cysteine since~~ it ~~resides~~ at ~~the dimer interface where the serine side chain interacts with the same residue in the opposite subunit~~. ~~Gel electrophoresis and X-ray crystallographic studies of the expressed mutant confirmed formation of the disulfide bond under nonreducing conditions~~. ~~However~~, the mutant protein was found to be less stable than the wild type as judged by susceptibility to denaturation in the presence of guanidine hydrochloride. Decreased stability probably results from formation of a disulfide bridge with a suboptimal torsion angle and exclusion of solvent molecules from the dimer interface.

The line below this paragraph, {{ABSTRACT_PUBMED_11747311}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11747311 is the PubMed ID number.

-->

==About this Structure==

Line 29:

Line 33:

[[Category: Iron]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 17~~:46:06 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:32:22 2008''

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1gn2.jpg|left|200px]]
+{{Seed}}
+[[Image:1gn2.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1gn2|  PDB=1gn2  |  SCENE=  }}
-'''S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.'''
+===S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.===
-==Overview==
+<!--
-With the aim of enhancing interactions involved in dimer formation, an intersubunit disulfide bridge was engineered in the superoxide dismutase enzyme of Mycobacterium tuberculosis. Ser-123 was chosen for mutation to cysteine since it resides at the dimer interface where the serine side chain interacts with the same residue in the opposite subunit. Gel electrophoresis and X-ray crystallographic studies of the expressed mutant confirmed formation of the disulfide bond under nonreducing conditions. However, the mutant protein was found to be less stable than the wild type as judged by susceptibility to denaturation in the presence of guanidine hydrochloride. Decreased stability probably results from formation of a disulfide bridge with a suboptimal torsion angle and exclusion of solvent molecules from the dimer interface.
+The line below this paragraph, {{ABSTRACT_PUBMED_11747311}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11747311 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11747311}}
 ==About this Structure==
@@ Line 29: / Line 33: @@
 [[Category: Iron]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:46:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 05:32:22 2008''