1w69: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,331,613 edits
No edit summary
Line 1: Line 1:
[[Image:1w69.gif|left|200px]]
{{Seed}}
[[Image:1w69.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1w69|  PDB=1w69  |  SCENE=  }}  
{{STRUCTURE_1w69|  PDB=1w69  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF MOUSE RIBONUCLEOTIDE REDUCTASE SUBUNIT R2 UNDER REDUCING CONDITIONS. A FULLY OCCUPIED DINUCLEAR IRON CLUSTER AND BOUND ACETATE.'''
===CRYSTAL STRUCTURE OF MOUSE RIBONUCLEOTIDE REDUCTASE SUBUNIT R2 UNDER REDUCING CONDITIONS. A FULLY OCCUPIED DINUCLEAR IRON CLUSTER AND BOUND ACETATE.===




==Overview==
<!--
Class I ribonucleotide reductase (RNR) catalyzes the de novo synthesis of deoxyribonucleotides in mammals and many other organisms. The RNR subunit R2 contains a dinuclear iron center, which in its diferrous form spontaneously reacts with O2, forming a mu-oxo-bridged diferric cluster and a stable tyrosyl radical. Here, we present the first crystal structures of R2 from mouse with its native dinuclear iron center, both under reducing and oxidizing conditions. In one structure obtained under reducing conditions, the iron-bridging ligand Glu-267 adopts the mu-(eta1,eta2) coordination mode, which has previously been related to O2 activation, and an acetate ion from the soaking solution is observed where O2 has been proposed to bind the iron. The structure of mouse R2 under oxidizing conditions resembles the nonradical diferric R2 from Escherichia coli, with the exception of the coordination of water and Asp-139 to Fe1. There are also additional water molecules near the tyrosyl radical site, as suggested by previous spectroscopic studies. Since no crystal structure of the active radical form has been reported, we propose models for the movement of waters and/or tyrosyl radical site when diferric R2 is oxidized to the radical form, in agreement with our previous ENDOR study. Compared with E. coli R2, two conserved phenylalanine residues in the hydrophobic environment around the diiron center have opposing rotameric conformations, and the carboxylate ligands of the diiron center in mouse R2 appear more flexible. Together, this might contribute to the lower affinity and cooperative binding of iron in mouse R2.
The line below this paragraph, {{ABSTRACT_PUBMED_15322079}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15322079 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15322079}}


==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Ribonucleotide reductase]]
[[Category: Ribonucleotide reductase]]
[[Category: Tyrosyl radical]]
[[Category: Tyrosyl radical]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:13:00 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:08:23 2008''

Revision as of 13:08, 27 July 2008

File:1w69.png

Template:STRUCTURE 1w69

CRYSTAL STRUCTURE OF MOUSE RIBONUCLEOTIDE REDUCTASE SUBUNIT R2 UNDER REDUCING CONDITIONS. A FULLY OCCUPIED DINUCLEAR IRON CLUSTER AND BOUND ACETATE.

Template:ABSTRACT PUBMED 15322079

About this Structure

1W69 is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structural studies of changes in the native dinuclear iron center of ribonucleotide reductase protein R2 from mouse., Strand KR, Karlsen S, Kolberg M, Rohr AK, Gorbitz CH, Andersson KK, J Biol Chem. 2004 Nov 5;279(45):46794-801. Epub 2004 Aug 17. PMID:15322079

Page seeded by OCA on Sun Jul 27 16:08:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1w69&oldid=655039"