2ckf
From Proteopedia
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| - | [[Image:2ckf.jpg|left|200px]]<br /><applet load="2ckf" size=" | + | [[Image:2ckf.jpg|left|200px]]<br /><applet load="2ckf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ckf, resolution 1.85Å" /> | caption="2ckf, resolution 1.85Å" /> | ||
'''CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1'''<br /> | '''CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CKF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sphingomonas_sp._chy-1 Sphingomonas sp. chy-1] with FE and FES as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Fe Binding Site For Chain E'>AC1</scene>. Full crystallographic information is available from [http:// | + | 2CKF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sphingomonas_sp._chy-1 Sphingomonas sp. chy-1] with <scene name='pdbligand=FE:'>FE</scene> and <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+E'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ring-hydroxylating dioxygenase]] | [[Category: ring-hydroxylating dioxygenase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:36:19 2008'' |
Revision as of 08:36, 3 February 2008
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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 Sphingomonas sp. chy-1 with and as ligands. Known structural/functional Site: . 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
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