2ckf

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[[Image:2ckf.jpg|left|200px]]
[[Image:2ckf.jpg|left|200px]]
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{{Structure
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|PDB= 2ckf |SIZE=350|CAPTION= <scene name='initialview01'>2ckf</scene>, resolution 1.85&Aring;
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The line below this paragraph, containing "STRUCTURE_2ckf", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+E'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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{{STRUCTURE_2ckf| PDB=2ckf | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ckf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ckf OCA], [http://www.ebi.ac.uk/pdbsum/2ckf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ckf RCSB]</span>
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}}
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'''CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1'''
'''CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1'''
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[[Category: Meyer, C.]]
[[Category: Meyer, C.]]
[[Category: Stojanoff, V.]]
[[Category: Stojanoff, V.]]
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[[Category: high-molecular-weight polycyclic aromatic hydrocarbon]]
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[[Category: High-molecular-weight polycyclic aromatic hydrocarbon]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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[[Category: pyrene dioxygenase]]
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[[Category: Pyrene dioxygenase]]
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[[Category: rieske non heme iron dioxygenase]]
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[[Category: Rieske non heme iron dioxygenase]]
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[[Category: ring-hydroxylating dioxygenase]]
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[[Category: Ring-hydroxylating dioxygenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:21:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:22:43 2008''
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Revision as of 19:21, 3 May 2008

Template:STRUCTURE 2ckf

CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1


Overview

Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme.

About this Structure

2CKF is a Protein complex structure of sequences from Bacteria. Full crystallographic information is available from OCA.

Reference

The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1., Jakoncic J, Jouanneau Y, Meyer C, Stojanoff V, Biochem Biophys Res Commun. 2007 Jan 26;352(4):861-6. Epub 2006 Dec 4. PMID:17157819 Page seeded by OCA on Sat May 3 22:21:15 2008

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