Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (26)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Stoddard, B. L.
Right arrow Articles by Petsko, G. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Stoddard, B. L.
Right arrow Articles by Petsko, G. A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering vol. 4 no. 2 pp. 113-119, 1990
© 1990 Oxford University Press

RESEARCH-ARTICLE

The structure of iron superoxide dismutase from Pseudomonas ovalis complexed with the inhibitor azide

Barry L. Stoddard1,2, Dagmar Ringe3 and Gregory A. Petsko3

Department of Chemistry, Massachusetts Institute of Technology Cambridge, MA 02139. USA 1Department of Biochemistry. Barker Hall. University of California Berkeley. CA 94720, USA 3Rosensteil Basic Medical Sciences Research Center, Room 650, Brandeis University Waltham, MA 02254, USA

2 To whom correspondence should be addressed

The 2.9 Å resolution structure of iron superoxide dismutase (FeSOD) (EC 1.15.1.1 [EC] ) from Pseudomonas ovalis complexed with the inhibitor azide was solved. Comparison of this structure with free enzyme shows that the inhibitor is bound at the open coordination position of the iron, with a bond length of 2.0 Å. The metal moves by 0.4 Å into the trigonal plane to produce an orthogonal geometry at the iron. Binding of the inhibitor also causes a movement of the axial ligand (histidine 26) away from the metal, a lengthening of the iron—histidine bond, and a rotation of the histidine 74 ring. The inhibitor possesses contacts in the binding pocket with a pair of conserved tryptophan residues and with the side chains of tyrosine 34 and glutamine 70. This glutamine is conserved between all FeSODs, but is absent in MnSOD. Comparisons with MnSOD show that a different glutamine which possesses the same interactions in the active site as Gln70 in FeSOD is conserved at position 154 in the overall SOD sequence, implying that while manganese and FeSODs are structural homologues in a global sense, their functional and evolutionary relationship is that of second-site mutation revertants.

Keywords: azide/iron/superoxide dismutase/X-ray crystallography

Received July 6, 1990; revised September 4, 1990; accepted September 11, 1990.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. M. Whittaker and J. W. Whittaker
A Glutamate Bridge Is Essential for Dimer Stability and Metal Selectivity in Manganese Superoxide Dismutase
J. Biol. Chem., August 28, 1998; 273(35): 22188 - 22193.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. L. Pinto, H. W. Hellinga, and J. P. Caradonna
Construction of a catalytically active iron superoxide dismutase by rational protein design
PNAS, May 27, 1997; 94(11): 5562 - 5567.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J.-L. Hsu, Y. Hsieh, C. Tu, D. O'Connor, H. S. Nick, and D. N. Silverman
Catalytic Properties of Human Manganese Superoxide Dismutase
J. Biol. Chem., July 26, 1996; 271(30): 17687 - 17691.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.