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1z8q

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[[Image:1z8q.jpg|left|200px]]
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{{STRUCTURE_1z8q| PDB=1z8q | SCENE= }}
{{STRUCTURE_1z8q| PDB=1z8q | SCENE= }}
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'''Ferrous dioxygen complex of the A245T cytochrome P450eryF'''
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===Ferrous dioxygen complex of the A245T cytochrome P450eryF===
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==Overview==
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Cytochrome P450eryF (CYP107A) from Saccaropolyspora ertherea catalyzes the hydroxylation of 6-deoxyerythronolide B, one of the early steps in the biosynthesis of erythromycin. P450eryF has an alanine rather than the conserved threonine that participates in the activation of dioxygen (O(2)) in most other P450s. The initial structure of P450eryF (Cupp-Vickery, J. R., Han, O., Hutchinson, C. R., and Poulos, T. L. (1996) Nat. Struct. Biol. 3, 632-637) suggests that the substrate 5-OH replaces the missing threonine OH group and holds a key active site water molecule in position to donate protons to the iron-linked dioxygen, a critical step for the monooxygenase reaction. To probe the proton delivery system in P450eryF, we have solved crystal structures of ferrous wild-type and mutant (Fe(2+)) dioxygen-bound complexes. The catalytic water molecule that was postulated to provide protons to dioxygen is absent, although the substrate 5-OH group donates a hydrogen bond to the iron-linked dioxygen. The hydrogen bond network observed in the wild-type ferrous dioxygen complex, water 63-Glu(360)-Ser(246)-water 53-Ala(241) carbonyl in the I-helix cleft, is proposed as the proton transfer pathway. Consistent with this view, the hydrogen bond network in the O(2).A245S and O(2) .A245T mutants, which have decreased or no enzyme activity, was perturbed or disrupted, respectively. The mutant Thr(245) side chain also perturbs the hydrogen bond between the substrate 5-OH and dioxygen ligand. Contrary to the previously proposed mechanism, these results support the direct involvement of the substrate in O(2) activation but raise questions on the role water plays as a direct proton donor to the iron-linked dioxygen.
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(as it appears on PubMed at http://www.pubmed.gov), where 15824115 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15824115}}
==About this Structure==
==About this Structure==
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[[Category: Heme]]
[[Category: Heme]]
[[Category: P450]]
[[Category: P450]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:19:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:33:22 2008''

Revision as of 19:34, 27 July 2008

Image:1z8q.png

Template:STRUCTURE 1z8q

Ferrous dioxygen complex of the A245T cytochrome P450eryF

Template:ABSTRACT PUBMED 15824115

About this Structure

1Z8Q is a Single protein structure of sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA.

Reference

Crystal structures of the ferrous dioxygen complex of wild-type cytochrome P450eryF and its mutants, A245S and A245T: investigation of the proton transfer system in P450eryF., Nagano S, Cupp-Vickery JR, Poulos TL, J Biol Chem. 2005 Jun 10;280(23):22102-7. Epub 2005 Apr 11. PMID:15824115

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