5y1i: Difference between revisions

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m Protected "5y1i" [edit=sysop:move=sysop]
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<StructureSection load='5y1i' size='340' side='right' caption='[[5y1i]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5y1i' size='340' side='right' caption='[[5y1i]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5y1i]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y1I FirstGlance]. <br>
<table><tr><td colspan='2'>[[5y1i]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1359 As 4.1359]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y1I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Y1I FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gfsF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68212 AS 4.1359])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5y1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y1i OCA], [http://pdbe.org/5y1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y1i RCSB], [http://www.ebi.ac.uk/pdbsum/5y1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y1i ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5y1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y1i OCA], [http://pdbe.org/5y1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5y1i RCSB], [http://www.ebi.ac.uk/pdbsum/5y1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5y1i ProSAT]</span></td></tr>
</table>
</table>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: As 4 1359]]
[[Category: Eguchi, T]]
[[Category: Eguchi, T]]
[[Category: Kudo, F]]
[[Category: Kudo, F]]

Revision as of 13:17, 15 November 2017

The crystal structure of GfsFThe crystal structure of GfsF

Structural highlights

5y1i is a 2 chain structure with sequence from As 4.1359. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:gfsF (AS 4.1359)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

GfsF is a multifunctional P450 monooxygenase that catalyzes the epoxidation and subsequent hydroxylation in the biosynthesis of macrolide polyketide FD-891. Here, we describe the biochemical and structural analysis of GfsF. To obtain the structural basis of a dual functional reaction, we determined the crystal structure of ligand-free GfsF, which revealed GfsF to have a predominantly hydrophobic substrate binding pocket. The docking models in conjunction with the results of the enzymatic assay with substrate analogs as well as site-directed mutagenesis suggested two distinct substrate binding modes for epoxidation and hydroxylation reactions, which explained how GfsF regulates the order of two oxidative reactions. These findings provide new insights into the reaction mechanism of multifunctional P450 monooxygenases.

Substrate recognition by a dual functional P450 monooxygenase GfsF involved in FD-891 biosynthesis.,Eguchi T, Miyanaga A, Takayanagi R, Furuya T, Kawamata A, Itagaki T, Iwabuchi Y, Kanoh N, Kudo F Chembiochem. 2017 Sep 4. doi: 10.1002/cbic.201700429. PMID:28869713[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Eguchi T, Miyanaga A, Takayanagi R, Furuya T, Kawamata A, Itagaki T, Iwabuchi Y, Kanoh N, Kudo F. Substrate recognition by a dual functional P450 monooxygenase GfsF involved in FD-891 biosynthesis. Chembiochem. 2017 Sep 4. doi: 10.1002/cbic.201700429. PMID:28869713 doi:http://dx.doi.org/10.1002/cbic.201700429

5y1i, resolution 2.00Å

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