3c3t

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_3c3t", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:3c3t.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:3c3t.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_3c3t| PDB=3c3t | SCENE= }}
{{STRUCTURE_3c3t| PDB=3c3t | SCENE= }}
-
'''Role of a Glutamate Bridge Spanning the Dimeric Interface of Human Manganese Superoxide Dismutase'''
+
===Role of a Glutamate Bridge Spanning the Dimeric Interface of Human Manganese Superoxide Dismutase===
-
==Overview==
+
<!--
-
The function in the structure, stability, and catalysis of the interfaces between subunits in manganese superoxide dismutase (MnSOD) is currently under scrutiny. Glu162 in homotetrameric human MnSOD spans a dimeric interface and forms a hydrogen bond with His163 of an adjacent subunit which is a direct ligand of the manganese. We have examined the properties of two site-specific mutants of human MnSOD in which Glu162 is replaced with Asp (E162D) and Ala (E162A). The X-ray crystal structures of E162D and E162A MnSOD reveal no significant structural changes compared with the wild type other than the removal of the hydrogen bond interaction with His163 in E162A MnSOD. In the case of E162D MnSOD, an intervening solvent molecule fills the void created by the mutation to conserve the hydrogen bond interaction between His163 and residue 162. These mutants retain their tetrameric structure and their specificity for manganese over iron. Each has catalytic activity in the disproportionation of superoxide that is typically 5-25% of that of the wild-type enzyme and a level of product inhibition greater by approximately 2-fold. Differential scanning calorimetry indicates that the hydrogen bond between Glu162 and His163 contributes to the stability of MnSOD, with the major unfolding transition occurring at 81 degrees C for E162A compared to 90 degrees C for wild-type MnSOD. These results suggest that Glu162 at the tetrameric interface in human MnSOD supports stability and efficient catalysis and has a significant role in regulating product inhibition.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18373354}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18373354 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_18373354}}
==About this Structure==
==About this Structure==
Line 36: Line 40:
[[Category: Polymorphism]]
[[Category: Polymorphism]]
[[Category: Transit peptide]]
[[Category: Transit peptide]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:51:42 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:51:41 2008''

Revision as of 00:51, 28 July 2008

Template:STRUCTURE 3c3t

Role of a Glutamate Bridge Spanning the Dimeric Interface of Human Manganese Superoxide Dismutase

Template:ABSTRACT PUBMED 18373354

About this Structure

3C3T is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Role of a Glutamate Bridge Spanning the Dimeric Interface of Human Manganese Superoxide Dismutase(,)., Quint PS, Domsic JF, Cabelli DE, McKenna R, Silverman DN, Biochemistry. 2008 Mar 29;. PMID:18373354

Page seeded by OCA on Mon Jul 28 03:51:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools