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.


1wb7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1wb7.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1wb7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1wb7| PDB=1wb7 | SCENE= }}
{{STRUCTURE_1wb7| PDB=1wb7 | SCENE= }}
-
'''IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE SULFOLOBUS SOLFATARICUS. CRYSTAL STRUCTURE OF THE Y41F MUTANT.'''
+
===IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE SULFOLOBUS SOLFATARICUS. CRYSTAL STRUCTURE OF THE Y41F MUTANT.===
-
==Overview==
+
<!--
-
We have examined and compared the effects of mutating Y41 and H155 in the iron superoxide dismutase (SOD) from the archaeon Sulfolobus solfataricus (Ss). These two neighboring residues in the active site are known to have crucial functions in structurally related SODs from different sources. The metal analysis indicates a slightly lower iron content after either Y41F or H155Q replacement, without any significant substitution of iron for manganese. The specific activity of SsSOD referred to the iron content is 17-fold reduced in the Y41F mutant, whereas it is less than 2-fold reduced by the H155Q mutation. The noticeable pH dependence of the activity of SsSOD and H155Q-SsSOD, due to the ionization of Y41 (pK 8.4), is lost in Y41F-SsSOD. After H155Q and even more after the Y41F substitution, the archaeal enzyme acquires a moderate sensitivity to sodium azide inhibition. The hydrogen peroxide inactivation of SsSOD is significantly increased after H155Q replacement; however, both mutants are insensitive to the modification of residue 41 by phenylmethanesulfonyl fluoride. Heat inactivation studies showed that the high stability of SsSOD is reduced by the H155Q mutation; however, upon the addition of SDS, a much faster inactivation kinetics is observed both with wild-type and mutant SsSOD forms. The detergent is also required to follow thermal denaturation of the archaeal enzyme by Fourier transform infrared spectroscopy; these studies gave information about the effect of mutations and modification on flexibility and compactness of the protein structure. The crystal structure of Y41F mutant revealed an uninterrupted hydrogen bond network including three solvent molecules connecting the iron-ligating hydroxide ion via H155 with F41 and H37, which is not present in structures of the corresponding mutant SODs from other sources. These data suggest that Y41 and H155 are important for the structural and functional properties of SsSOD; in particular, Y41 seems to be a powerful regulator of the activity of SsSOD, whereas H155 is apparently involved in the organization of the active site of the enzyme.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14979716}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14979716 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14979716}}
==About this Structure==
==About this Structure==
Line 37: Line 41:
[[Category: Superoxide radical disproportionation]]
[[Category: Superoxide radical disproportionation]]
[[Category: Thermostable]]
[[Category: Thermostable]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:24:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:42:07 2008''

Revision as of 14:42, 28 July 2008

Image:1wb7.png

Template:STRUCTURE 1wb7

IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE SULFOLOBUS SOLFATARICUS. CRYSTAL STRUCTURE OF THE Y41F MUTANT.

Template:ABSTRACT PUBMED 14979716

About this Structure

1WB7 is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.

Reference

The role of Tyr41 and His155 in the functional properties of superoxide dismutase from the archaeon Sulfolobus solfataricus., Gogliettino MA, Tanfani F, Scire A, Ursby T, Adinolfi BS, Cacciamani T, De Vendittis E, Biochemistry. 2004 Mar 2;43(8):2199-208. PMID:14979716

Page seeded by OCA on Mon Jul 28 17:42:07 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wb7"
Personal tools