1o7w

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 31: Line 31:
[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:12:19 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 16:46:00 2007''

Revision as of 14:40, 5 November 2007


1o7w, resolution 1.90Å

Drag the structure with the mouse to rotate

NAPHTHALENE 1,2-DIOXYGENASE, FULLY REDUCED FORM

Overview

Binding of oxygen to iron is exploited in several biological and chemical, processes. Although computational and spectroscopic results have suggested, side-on binding, only end-on binding of oxygen to iron has been observed, in crystal structures. We have determined structures of naphthalene, dioxygenase that show a molecular oxygen species bound to the mononuclear, iron in a side-on fashion. In a complex with substrate and dioxygen, the, dioxygen molecule is lined up for an attack on the double bond of the, aromatic substrate. The structures reported here provide the basis for a, reaction mechanism and for the high stereospecificity of the reaction, catalyzed by naphthalene dioxygenase.

About this Structure

1O7W is a Protein complex structure of sequences from Pseudomonas putida with SO4, FE, EDO and FES as ligands. Active as Naphthalene 1,2-dioxygenase, with EC number 1.14.12.12 Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron., Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S, Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937

Page seeded by OCA on Mon Nov 5 16:46:00 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools