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1egy

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Revision as of 05:21, 10 September 2015

CYTOCHROME P450ERYF WITH 9-AMINOPHENANTHRENE BOUND

Structural highlights

1egy is a 1 chain structure with sequence from Saccharopolyspora erythraea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1oxa
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CPXJ_SACEN] Catalyzes the NADPH-dependent conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Several mammalian cytochrome P450 (P450) isoforms demonstrate homotropic cooperativity with a number of substrates, including steroids and polycyclic aromatic hydrocarbons. To identify structural factors contributing to steroid and polycyclic aromatic hydrocarbon binding to P450 enzymes and to determine the location of the allosteric site, we investigated interactions of the macrolide hydroxylase P450eryF from Saccharopolyspora erythraea with androstenedione and 9-aminophenanthrene. Spectroscopic binding assays indicate that P450eryF binds androstenedione with an affinity of 365 microM and a Hill coefficient of 1.31 +/- 0.6 and coordinates with 9-aminophenanthrene with an affinity of 91 microM and a Hill coefficient of 1.38 +/- 0.2. Crystals of complexes of androstenedione and 9-aminophenanthrene with P450eryF were grown and diffracted to 2.1 A and 2.35 A, respectively. Electron density maps indicate that for both complexes two ligand molecules are simultaneously present in the active site. The P450eryF/androstenedione model was refined to an r = 18.9%, and the two androstenedione molecules have similar conformations. The proximal androstenedione is positioned such that the alpha-face of carbon-6 is closest to the heme iron, and the second steroid molecule is positioned 5.5 A distal in the active site. The P450eryF/9-aminophenanthrene model was refined to an r = 19.7% with the proximal 9-aminophenanthrene coordinated with the heme iron through the 9-amino group and the second ligand positioned approximately 6 A distal in the active site. These results establish that homotropic cooperativity in ligand binding can result from binding of two substrate molecules within the active site pocket without major conformational changes in the protein.

Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity.,Cupp-Vickery J, Anderson R, Hatziris Z Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3050-5. PMID:10716705^[3]

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

References

↑ Andersen JF, Hutchinson CR. Characterization of Saccharopolyspora erythraea cytochrome P-450 genes and enzymes, including 6-deoxyerythronolide B hydroxylase. J Bacteriol. 1992 Feb;174(3):725-35. PMID:1732208
↑ Weber JM, Leung JO, Swanson SJ, Idler KB, McAlpine JB. An erythromycin derivative produced by targeted gene disruption in Saccharopolyspora erythraea. Science. 1991 Apr 5;252(5002):114-7. PMID:2011746
↑ Cupp-Vickery J, Anderson R, Hatziris Z. Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3050-5. PMID:10716705 doi:http://dx.doi.org/10.1073/pnas.050406897

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1egy"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9AP:9-AMINOPHENANTHRENE'>9AP</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oxa|1oxa]]</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=1egy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1egy RCSB], [http://www.ebi.ac.uk/pdbsum/1egy PDBsum]</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=1egy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egy OCA], [http://pdbe.org/1egy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1egy RCSB], [http://www.ebi.ac.uk/pdbsum/1egy PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CPXJ_SACER CPXJ_SACER]] Conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB.
+[[http://www.uniprot.org/uniprot/CPXJ_SACEN CPXJ_SACEN]] Catalyzes the NADPH-dependent conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase.<ref>PMID:1732208</ref> <ref>PMID:2011746</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1egy" style="background-color:#fffaf0;"></div>
 ==See Also==

1egy

From Proteopedia

Revision as of 05:21, 10 September 2015

CYTOCHROME P450ERYF WITH 9-AMINOPHENANTHRENE BOUND

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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