3eln

A Putative Fe2+-bound Persulfenate Intermediate in Cysteine Dioxygenase

spinqualitylabelsall models 3eln, resolution 1.42Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3eln is a 1 chain structure with sequence from Buffalo rat. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 2CO, FE2 Related: 2b5h, 2gh2 Gene: Cdo1 (Buffalo rat) Activity: Cysteine dioxygenase, with EC number 1.13.11.20 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The common reactions of dioxygen, superoxide, and hydroperoxides with thiolates are thought to proceed via persulfenate intermediates, yet these have never been visualized. Here we report a 1.4 A resolution crystal structure of the Fe(2+)-dependent enzyme cysteine dioxygenase (CDO) containing this putative intermediate trapped in its active site pocket. The complex raises the possibility that, distinct from known dioxygenases and proposed CDO mechanisms, the Fe-proximal oxygen atom may be involved in the primary oxidation event yielding a unique three-membered Fe-S-O cyclic intermediate. A nonpolar environment of the distal oxygen would facilitate isomerization of the persulfenate to the sulfinate product. A putative Fe2+-bound persulfenate intermediate in cysteine dioxygenase.,Simmons CR, Krishnamoorthy K, Granett SL, Schuller DJ, Dominy JE Jr, Begley TP, Stipanuk MH, Karplus PA Biochemistry. 2008 Nov 4;47(44):11390-2. Epub 2008 Oct 11. PMID:18847220 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dioxygenase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA