2x80

From Proteopedia

(Difference between revisions)

Revision as of 07:06, 5 August 2016

P450 BM3 F87A in complex with DMSO

Structural highlights

2x80 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:	, ,
Related:	1p0v, 1fag, 1smi, 2j1m, 1jme, 2x7y, 1smj, 2j4s, 2hpd, 1bvy, 1bu7, 1yqp, 2uwh, 2bmh, 1jpz, 1yqo, 1p0x, 1fah, 1p0w
Activity:	Unspecific monooxygenase, with EC number 1.14.14.1
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

Understanding the effects of organic co-solvents on protein structure and function is pivotal to engineering enzymes for biotransformation in non-aqueous solvents. The effects of DMSO on the catalytic activity of cytochrome P450 BM3 have previously been investigated and the importance of Phe87 in its organic co-solvent tolerance was identified. To probe the DMSO inactivation mechanism and the functional role of Phe87 in modulating the organic co-solvent tolerance of P450 BM3, the haem domain (Thr1-Leu455) of the F87A variant was cocrystallized in the presence of 14%(v/v) and 28%(v/v) DMSO. At both DMSO concentrations the protein retained the canonical structure of the P450 haem domain without any sign of partial or global unfolding. Interestingly, a DMSO molecule was found in the active site of both structures, with its O atom pointing towards the haem iron. The orientation of the DMSO molecule indicated a dynamic coordination process that was in competition with the active-site water molecule. The ability of the DMSO molecule to coordinate the haem iron is plausibly the main reason why P450 BM3 is inactivated at elevated DMSO concentrations. The data allowed an interesting comparison with the wild-type structures reported previously. A DMSO molecule was found when the wild-type protein was placed in 28%(v/v) DMSO, in which the DMSO molecule coordinated the haem iron directly via its S atom. Intriguingly, no DMSO molecule was observed at 14%(v/v) DMSO for the wild-type structure. These results suggested that the bulky phenyl side chain of Phe87 protects the haem from being accessed by the DMSO molecule and explains the higher tolerance of the wild-type enzyme towards organic co-solvents compared with its F87A variant.

The role of active-site Phe87 in modulating the organic co-solvent tolerance of cytochrome P450 BM3 monooxygenase.,Kuper J, Tee KL, Wilmanns M, Roccatano D, Schwaneberg U, Wong TS Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Sep;68(Pt 9):1013-7. Epub , 2012 Aug 29. PMID:22949185^[1]

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

References

↑ Kuper J, Tee KL, Wilmanns M, Roccatano D, Schwaneberg U, Wong TS. The role of active-site Phe87 in modulating the organic co-solvent tolerance of cytochrome P450 BM3 monooxygenase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Sep;68(Pt 9):1013-7. Epub , 2012 Aug 29. PMID:22949185 doi:http://dx.doi.org/10.1107/S1744309112031570

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/2x80"

@@ Line 1: / Line 1: @@
 ==P450 BM3 F87A in complex with DMSO==
 <StructureSection load='2x80' size='340' side='right' caption='[[2x80]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2x80]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X80 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X80 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2x80]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14581 Atcc 14581]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X80 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X80 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1p0v|1p0v]], [[1fag|1fag]], [[1smi|1smi]], [[2j1m|2j1m]], [[1jme|1jme]], [[2x7y|2x7y]], [[1smj|1smj]], [[2j4s|2j4s]], [[2hpd|2hpd]], [[1bvy|1bvy]], [[1bu7|1bu7]], [[1yqp|1yqp]], [[2uwh|2uwh]], [[2bmh|2bmh]], [[1jpz|1jpz]], [[1yqo|1yqo]], [[1p0x|1p0x]], [[1fah|1fah]], [[1p0w|1p0w]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Unspecific_monooxygenase Unspecific monooxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.14.1 1.14.14.1] </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=2x80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x80 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2x80 RCSB], [http://www.ebi.ac.uk/pdbsum/2x80 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=2x80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x80 OCA], [http://pdbe.org/2x80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x80 RCSB], [http://www.ebi.ac.uk/pdbsum/2x80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x80 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2x80" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 25: / Line 27: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus megaterium]]
+[[Category: Atcc 14581]]
 [[Category: Unspecific monooxygenase]]
 [[Category: Kuper, J]]

2x80

From Proteopedia

Revision as of 07:06, 5 August 2016

P450 BM3 F87A in complex with DMSO

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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