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[[Image:2fae.gif|left|200px]]<br /><applet load="2fae" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2fae, resolution 1.550&Aring;" />
'''Crystal structure of E. coli decanoyl-ACP'''<br />


==Overview==
==Crystal structure of E. coli decanoyl-ACP==
<StructureSection load='2fae' size='340' side='right'caption='[[2fae]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2fae]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. The June 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Fatty Acid Synthase''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_6 10.2210/rcsb_pdb/mom_2007_6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FAE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FAE 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]] 1.55&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PM8:S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL)+DECANETHIOATE'>PM8</scene>, <scene name='pdbligand=PSE:O-PHOSPHOETHANOLAMINE'>PSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2fae FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fae OCA], [https://pdbe.org/2fae PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fae RCSB], [https://www.ebi.ac.uk/pdbsum/2fae PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fae ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACP_ECOLI ACP_ECOLI] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217]
== 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/fa/2fae_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2fae ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A knowledge of the structures of acyl chain loaded species of the acyl carrier protein (ACP) as used in fatty acid biosynthesis and a range of other metabolic events, is essential for a full understanding of the molecular recognition at the heart of these processes. To date the only crystal structure of an acylated species of ACP is that of a butyryl derivative of Escherichia coli ACP. We have now determined the structures of a family of acylated E. coli ACPs of varying acyl chain length. The acyl moiety is attached via a thioester bond to a phosphopantetheine linker that is in turn bound to a serine residue in ACP. The growing acyl chain can be accommodated within a central cavity in the ACP for transport during the elongation stages of lipid synthesis through changes in the conformation of a four alpha-helix bundle. The results not only clarify the means by which a substrate of varying size and complexity is transported in the cell but also suggest a mechanism by which interacting enzymes can recognize the loaded ACP through recognition of surface features including the conformation of the phosphopantetheine linker.
A knowledge of the structures of acyl chain loaded species of the acyl carrier protein (ACP) as used in fatty acid biosynthesis and a range of other metabolic events, is essential for a full understanding of the molecular recognition at the heart of these processes. To date the only crystal structure of an acylated species of ACP is that of a butyryl derivative of Escherichia coli ACP. We have now determined the structures of a family of acylated E. coli ACPs of varying acyl chain length. The acyl moiety is attached via a thioester bond to a phosphopantetheine linker that is in turn bound to a serine residue in ACP. The growing acyl chain can be accommodated within a central cavity in the ACP for transport during the elongation stages of lipid synthesis through changes in the conformation of a four alpha-helix bundle. The results not only clarify the means by which a substrate of varying size and complexity is transported in the cell but also suggest a mechanism by which interacting enzymes can recognize the loaded ACP through recognition of surface features including the conformation of the phosphopantetheine linker.


==About this Structure==
Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates.,Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR J Mol Biol. 2007 Jan 5;365(1):135-45. Epub 2006 Sep 23. PMID:17059829<ref>PMID:17059829</ref>
2FAE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=PM8:'>PM8</scene> and <scene name='pdbligand=PSE:'>PSE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 2FAE with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FAE OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural studies of fatty acyl-(acyl carrier protein) thioesters reveal a hydrophobic binding cavity that can expand to fit longer substrates., Roujeinikova A, Simon WJ, Gilroy J, Rice DW, Rafferty JB, Slabas AR, J Mol Biol. 2007 Jan 5;365(1):135-45. Epub 2006 Sep 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17059829 17059829]
</div>
<div class="pdbe-citations 2fae" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Fatty Acid Synthase]]
[[Category: Fatty Acid Synthase]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Roujeinikova, A.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: PM8]]
[[Category: Roujeinikova A]]
[[Category: PSE]]
[[Category: ZN]]
[[Category: acyl carrier protein]]
[[Category: acyl chain binding]]
[[Category: fatty acid biosynthesis]]
 
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