1pn0
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(New page: 200px<br /><applet load="1pn0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pn0, resolution 1.70Å" /> '''Phenol hydroxylase f...)
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Revision as of 21:48, 20 November 2007
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Phenol hydroxylase from Trichosporon cutaneum
Overview
The crystal structure model of phenol hydroxylase has been corrected for, 11 sequence errors and refined against new data to 1.7 A resolution. The, higher resolution data together with careful exploitation of, non-crystallographic symmetry restraints and the use of many small groups, for refinement of anisotropic displacement parameters resulted in a large, decrease in the crystallographic R factor. The final crystallographic free, R factor is 18.0%, which should be compared with the values of 27.8% for, the previously published model (PDB code 1foh). The rebuilding and, re-refinement procedure is described. A comparison with the previously, published model was performed and possible biochemical implications are, discussed. No large differences suggesting gross errors in the earlier, model were found. The actual differences between these two models give an, indication of the level of ambiguity and inaccuracy that may be found in a, well refined protein model at 2.4 A resolution.
About this Structure
1PN0 is a Single protein structure of sequence from Trichosporon cutaneum with CL, FAD and IPH as ligands. Active as Phenol 2-monooxygenase, with EC number 1.14.13.7 Full crystallographic information is available from OCA.
Reference
High-resolution structure of phenol hydroxylase and correction of sequence errors., Enroth C, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1597-602. Epub 2003, Aug 19. PMID:12925790
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