3ejb

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[[Image:3ejb.png|left|200px]]
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==Crystal Structure of P450BioI in complex with tetradecanoic acid ligated Acyl Carrier Protein==
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<StructureSection load='3ejb' size='340' side='right' caption='[[3ejb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ejb]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EJB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EJB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HTG:HEPTYL+1-THIOHEXOPYRANOSIDE'>HTG</scene>, <scene name='pdbligand=ZMP:({(3S)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-[(3-OXO-3-{[2-(TETRADECANOYLSULFANYL)ETHYL]AMINO}PROPYL)AMINO]BUTYL}OXY)(OXO)PHOSPHONIUMOLATE'>ZMP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ejd|3ejd]], [[3eje|3eje]]</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acpP, b1094, JW1080 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), bioI, CYP107H, BSU30190 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr>
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<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=3ejb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ejb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ejb RCSB], [http://www.ebi.ac.uk/pdbsum/3ejb PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ACP_ECOLI ACP_ECOLI]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] [[http://www.uniprot.org/uniprot/BIOI_BACSU BIOI_BACSU]] Catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. It has high affinity for long-chain fatty acids with the greatest affinity for myristic acid.<ref>PMID:8763940</ref> <ref>PMID:11368323</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ej/3ejb_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cytochrome P450(BioI) (CYP107H1) from the biotin operon of Bacillus subtilis forms a seven-carbon diacid through a multistep oxidative cleavage of a fatty acid linked to acyl carrier protein (ACP). Crystal structures of P450(BioI) in complex with three different length fatty acyl-ACP (Escherichia coli) ligands show that P450(BioI) binds the fatty acid such as to force the carbon chain into a U-shape above the active site heme. This positions the C7 and C8 carbons for oxidation, with a large additional cavity extending beyond the heme to accommodate the methyl termini of fatty acids beyond the site of cleavage. The structures explain the experimentally observed lack of stereo- and regiospecificity in the hydroxylation and cleavage of free fatty acids. The P450(BioI)-ACP complexes represent the only structurally characterized P450-carrier protein complexes to date, which has allowed the generation of a model of the interaction of the vancomycin biosynthetic P450 OxyB with its proposed carrier protein bound substrate.
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{{STRUCTURE_3ejb| PDB=3ejb | SCENE= }}
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Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI) ACP complex.,Cryle MJ, Schlichting I Proc Natl Acad Sci U S A. 2008 Oct 14;105(41):15696-701. Epub 2008 Oct 6. PMID:18838690<ref>PMID:18838690</ref>
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===Crystal Structure of P450BioI in complex with tetradecanoic acid ligated Acyl Carrier Protein===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_18838690}}
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==About this Structure==
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[[3ejb]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EJB OCA].
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==See Also==
==See Also==
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*[[Acyl carrier protein|Acyl carrier protein]]
*[[Fatty acid synthase|Fatty acid synthase]]
*[[Fatty acid synthase|Fatty acid synthase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:018838690</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Cryle, M J.]]
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[[Category: Cryle, M J]]
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[[Category: Schlichting, I.]]
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[[Category: Schlichting, I]]
[[Category: 4-helix bundle]]
[[Category: 4-helix bundle]]
[[Category: Biotin biosynthesis]]
[[Category: Biotin biosynthesis]]

Revision as of 04:21, 25 December 2014

Crystal Structure of P450BioI in complex with tetradecanoic acid ligated Acyl Carrier Protein

3ejb, resolution 2.00Å

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