4dqk

From Proteopedia

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Revision as of 23:35, 4 August 2016

Crystal structure of the FAD binding domain of cytochrome P450 BM3

Structural highlights

4dqk is a 2 chain structure with sequence from Atcc 14581. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	CYP102A1, cyp102 (ATCC 14581)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CPXB_BACME] Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of medium and long-chain fatty acids at omega-1, omega-2 and omega-3 positions, with optimum chain lengths of 12-16 carbons (lauric, myristic, and palmitic acids). The reductase domain is required for electron transfer from NADP to cytochrome P450.

Publication Abstract from PubMed

We report the crystal structure of the FAD/NADPH-binding domain of the biotechnologically important flavocytochrome P450 BM3, the last domain of the enzyme to be structurally resolved. The structure was solved in both absence and presence of the ligand NADP(+) , identifying important protein interactions with the NADPH 2'-phosphate that help to dictate specificity for NADPH over NADH, and involving residues Tyr974, Arg966, Lys972 and Ser965. The Trp1046 side chain shields the FAD isoalloxazine ring from NADPH, and motion of this residue is required to enable NADPH-dependent FAD reduction. Multiple binding interactions stabilize the FAD cofactor, including aromatic stacking with the adenine group from the side chains of Tyr860 and Trp854, and several interactions with FAD pyrophosphate oxygens, including bonding to tyrosines 828, 829 and 860. Mutagenesis of C773 and C999 to alanine was required for successful crystallization, with C773A predicted to disfavour intramolecular and intermolecular disulfide bonding. Multi-angle laser light scattering analysis showed wild-type FAD domain to be near-exclusively dimeric, with dimer disruption achieved on treatment with the reducing agent dithiothreitol. In contrast, light scattering showed that the C773A/C999A FAD domain was monomeric. The C773A/C999A FAD domain structure confirms that Ala773 is surface exposed and in close proximity to Cys810, with this region of the enzyme's connecting domain (that links the FAD domain to the FMN-binding domain in P450 BM3) located at a crystal contact interface between FAD domains. The FAD/NADPH domain crystal structure enables molecular modelling of its interactions with its cognate FMN (flavodoxin-like) domain within the BM3 reductase module.

The crystal structure of the FAD/NADPH binding domain of flavocytochrome P450 BM3.,Gordon Joyce M, Ekanem IS, Roitel O, Dunford AJ, Neeli R, Girvan HM, Baker GJ, Curtis RA, Munro AW, Leys D FEBS J. 2012 Feb 22. doi: 10.1111/j.1742-4658.2012.08544.x. PMID:22356131^[1]

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

References

↑ Gordon Joyce M, Ekanem IS, Roitel O, Dunford AJ, Neeli R, Girvan HM, Baker GJ, Curtis RA, Munro AW, Leys D. The crystal structure of the FAD/NADPH binding domain of flavocytochrome P450 BM3. FEBS J. 2012 Feb 22. doi: 10.1111/j.1742-4658.2012.08544.x. PMID:22356131 doi:10.1111/j.1742-4658.2012.08544.x

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4dqk"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the FAD binding domain of cytochrome P450 BM3==
 <StructureSection load='4dqk' size='340' side='right' caption='[[4dqk]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP102A1, cyp102 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 ATCC 14581])</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=4dqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dqk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dqk RCSB], [http://www.ebi.ac.uk/pdbsum/4dqk 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=4dqk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dqk OCA], [http://pdbe.org/4dqk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dqk RCSB], [http://www.ebi.ac.uk/pdbsum/4dqk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dqk ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4dqk" style="background-color:#fffaf0;"></div>
 ==See Also==

4dqk

From Proteopedia

Revision as of 23:35, 4 August 2016

Crystal structure of the FAD binding domain of cytochrome P450 BM3

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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