2ckf: Difference between revisions
New page: left|200px<br /> <applet load="2ckf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ckf, resolution 1.85Å" /> '''CRYSTAL STRUCTURE O... |
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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]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CKF OCA]]. | 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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.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://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:36:11 2007'' | ||
Revision as of 15:31, 30 October 2007
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CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1
OverviewOverview
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 StructureAbout this Structure
2CKF is a [Protein complex] structure of sequences from [Sphingomonas sp. chy-1] with FE and FES as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
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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