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[[Image:2ca0.gif|left|200px]]<br />
<applet load="2ca0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2ca0, resolution 2.85&Aring;" />
'''CRYSTAL STRUCTURE OF YC-17-BOUND CYTOCHROME P450 PIKC (CYP107L1)'''<br />


==About this Structure==
==Crystal structure of YC-17-bound cytochrome P450 PikC (CYP107L1)==
2CA0 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]] with HEM and PXI as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CA0 OCA]].
<StructureSection load='2ca0' size='340' side='right'caption='[[2ca0]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
[[Category: Single protein]]
== Structural highlights ==
<table><tr><td colspan='2'>[[2ca0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_venezuelae Streptomyces venezuelae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CA0 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PXI:4-{[4-(DIMETHYLAMINO)-3-HYDROXY-6-METHYLTETRAHYDRO-2H-PYRAN-2-YL]OXY}-12-ETHYL-3,5,7,11-TETRAMETHYLOXACYCLODODEC-9-ENE-2,8-DIONE'>PXI</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ca0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ca0 OCA], [https://pdbe.org/2ca0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ca0 RCSB], [https://www.ebi.ac.uk/pdbsum/2ca0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ca0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PIKC_STRVZ PIKC_STRVZ] Catalyzes the hydroxylation of narbomycin to give rise to pikromycin, and of 10-deoxymethymycin (YC-17) to give rise to methymycin and neomethymycin during macrolide antibiotic biosynthesis. In addition, produces low amounts of neopicromycin, novapikromycin and novamethymycin. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase.<ref>PMID:16825192</ref> <ref>PMID:19124459</ref> <ref>PMID:19833867</ref> <ref>PMID:24627965</ref> <ref>PMID:9778370</ref> <ref>PMID:9831532</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ca/2ca0_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ca0 ConSurf].
<div style="clear:both"></div>
 
==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
*[[Cytochrome P450 hydroxylase 3D structures|Cytochrome P450 hydroxylase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Streptomyces venezuelae]]
[[Category: Streptomyces venezuelae]]
[[Category: Kim, Y.]]
[[Category: Kim Y]]
[[Category: Podust, L.M.]]
[[Category: Podust LM]]
[[Category: Sherman, D.H.]]
[[Category: Sherman DH]]
[[Category: Waterman, M.R.]]
[[Category: Waterman MR]]
[[Category: Yermalitskaya, L.I.]]
[[Category: Yermalitskaya LI]]
[[Category: HEM]]
[[Category: PXI]]
[[Category: antibiotic biosynthesis]]
[[Category: cytochrome p450]]
[[Category: heme]]
[[Category: iron]]
[[Category: macrolide monooxygenase]]
[[Category: metal-binding]]
[[Category: oxidoreductase]]
[[Category: pikc]]
[[Category: yc-17]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:31:50 2007''

Latest revision as of 17:11, 13 December 2023

Crystal structure of YC-17-bound cytochrome P450 PikC (CYP107L1)Crystal structure of YC-17-bound cytochrome P450 PikC (CYP107L1)

Structural highlights

2ca0 is a 2 chain structure with sequence from Streptomyces venezuelae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.85Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PIKC_STRVZ Catalyzes the hydroxylation of narbomycin to give rise to pikromycin, and of 10-deoxymethymycin (YC-17) to give rise to methymycin and neomethymycin during macrolide antibiotic biosynthesis. In addition, produces low amounts of neopicromycin, novapikromycin and novamethymycin. Requires the participation of a ferredoxin and a ferredoxin reductase for the transfer of electrons from NADPH to the monooxygenase.[1] [2] [3] [4] [5] [6]

Evolutionary Conservation

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

See Also

References

  1. ↑ Sherman DH, Li S, Yermalitskaya LV, Kim Y, Smith JA, Waterman MR, Podust LM. The structural basis for substrate anchoring, active site selectivity, and product formation by P450 PikC from Streptomyces venezuelae. J Biol Chem. 2006 Sep 8;281(36):26289-97. Epub 2006 Jul 6. PMID:16825192 doi:10.1074/jbc.M605478200
  2. ↑ Li S, Ouellet H, Sherman DH, Podust LM. Analysis of transient and catalytic desosamine-binding pockets in cytochrome P-450 PikC from Streptomyces venezuelae. J Biol Chem. 2009 Feb 27;284(9):5723-30. Epub 2009 Jan 4. PMID:19124459 doi:10.1074/jbc.M807592200
  3. ↑ Li S, Chaulagain MR, Knauff AR, Podust LM, Montgomery J, Sherman DH. Selective oxidation of carbolide C-H bonds by an engineered macrolide P450 mono-oxygenase. Proc Natl Acad Sci U S A. 2009 Oct 15. PMID:19833867
  4. ↑ Negretti S, Narayan AR, Chiou KC, Kells PM, Stachowski JL, Hansen DA, Podust LM, Montgomery J, Sherman DH. Directing Group-Controlled Regioselectivity in an Enzymatic C-H Bond Oxygenation. J Am Chem Soc. 2014 Mar 21. PMID:24627965 doi:http://dx.doi.org/10.1021/ja5016052
  5. ↑ Betlach MC, Kealey JT, Ashley GW, McDaniel R. Characterization of the macrolide P-450 hydroxylase from Streptomyces venezuelae which converts narbomycin to picromycin. Biochemistry. 1998 Oct 20;37(42):14937-42. PMID:9778370 doi:10.1021/bi981699c
  6. ↑ Xue Y, Wilson D, Zhao L, Liu Hw, Sherman DH. Hydroxylation of macrolactones YC-17 and narbomycin is mediated by the pikC-encoded cytochrome P450 in Streptomyces venezuelae. Chem Biol. 1998 Nov;5(11):661-7. PMID:9831532 doi:10.1016/s1074-5521(98)90293-9

2ca0, resolution 2.85Å

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