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[[Image: | ==NMR solution structures of 3-oxooctanyl-ACP from Streptomyces coelicolor Fatty Acid Synthase== | ||
<StructureSection load='2kop' size='340' side='right' caption='[[2kop]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2kop]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KOP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SYO:[(3S)-3-HYDROXY-2,2-DIMETHYL-4-OXO-4-[[3-OXO-3-[2-(3-OXOOCTYLSULFANYL)ETHYLAMINO]PROPYL]AMINO]BUTYL]+DIHYDROGEN+PHOSPHATE'>SYO</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2koo|2koo]], [[2koq|2koq]], [[2kor|2kor]], [[2kos|2kos]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acpP, SCO2389, SC4A7.17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1902 Streptomyces coelicolor])</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=2kop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kop OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2kop RCSB], [http://www.ebi.ac.uk/pdbsum/2kop PDBsum]</span></td></tr> | |||
</table> | |||
== 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/ko/2kop_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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
It remains unclear whether in a bacterial fatty acid synthase (FAS) acyl chain transfer is a programmed or diffusion controlled and random action. Acyl carrier protein (ACP), which delivers all intermediates and interacts with all synthase enzymes, is the key player in this process. High-resolution structures of intermediates covalently bound to an ACP representing each step in fatty acid biosynthesis have been solved by solution NMR. These include hexanoyl-, 3-oxooctanyl-, 3R-hydroxyoctanoyl-, 2-octenoyl-, and octanoyl-ACP from Streptomyces coelicolor FAS. The high-resolution structures reveal that the ACP adopts a unique conformation for each intermediate driven by changes in the internal fatty acid binding pocket. The binding of each intermediate shows conserved structural features that may ensure effective molecular recognition over subsequent rounds of fatty acid biosynthesis. | |||
Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis.,Ploskon E, Arthur CJ, Kanari AL, Wattana-amorn P, Williams C, Crosby J, Simpson TJ, Willis CL, Crump MP Chem Biol. 2010 Jul 30;17(7):776-85. PMID:20659690<ref>PMID:20659690</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Acyl carrier protein|Acyl carrier protein]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
== | </StructureSection> | ||
< | |||
[[Category: Streptomyces coelicolor]] | [[Category: Streptomyces coelicolor]] | ||
[[Category: Arthur, C J.]] | [[Category: Arthur, C J.]] | ||
Revision as of 18:39, 12 October 2014
NMR solution structures of 3-oxooctanyl-ACP from Streptomyces coelicolor Fatty Acid SynthaseNMR solution structures of 3-oxooctanyl-ACP from Streptomyces coelicolor Fatty Acid Synthase
Structural highlights
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 PubMedIt remains unclear whether in a bacterial fatty acid synthase (FAS) acyl chain transfer is a programmed or diffusion controlled and random action. Acyl carrier protein (ACP), which delivers all intermediates and interacts with all synthase enzymes, is the key player in this process. High-resolution structures of intermediates covalently bound to an ACP representing each step in fatty acid biosynthesis have been solved by solution NMR. These include hexanoyl-, 3-oxooctanyl-, 3R-hydroxyoctanoyl-, 2-octenoyl-, and octanoyl-ACP from Streptomyces coelicolor FAS. The high-resolution structures reveal that the ACP adopts a unique conformation for each intermediate driven by changes in the internal fatty acid binding pocket. The binding of each intermediate shows conserved structural features that may ensure effective molecular recognition over subsequent rounds of fatty acid biosynthesis. Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis.,Ploskon E, Arthur CJ, Kanari AL, Wattana-amorn P, Williams C, Crosby J, Simpson TJ, Willis CL, Crump MP Chem Biol. 2010 Jul 30;17(7):776-85. PMID:20659690[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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