1kas: Difference between revisions

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New page: left|200px<br /> <applet load="1kas" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kas, resolution 2.4Å" /> '''BETA-KETOACYL-ACP SY...
 
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[[Image:1kas.gif|left|200px]]<br />
<applet load="1kas" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1kas, resolution 2.4&Aring;" />
'''BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI'''<br />


==Overview==
==BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI==
In the biosynthesis of fatty acids, the beta-ketoacyl-acyl carrier protein, (ACP) synthases catalyze chain elongation by the addition of two-carbon, units derived from malonyl-ACP to an acyl group bound to either ACP or, CoA. The crystal structure of beta-ketoacyl synthase II from Escherichia, coli has been determined with the multiple isomorphous replacement method, and refined at 2.4 A resolution. The subunit consists of two mixed, five-stranded beta-sheets surrounded by alpha-helices. The two sheets are, packed against each other in such a way that the fold can be described as, consisting of five layers, alpha-beta-alpha-beta-alpha. The enzyme is a, homodimer, and the subunits are related by a crystallographic 2-fold axis., The two active sites are located near the dimer interface but ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9482715 (full description)]]
<StructureSection load='1kas' size='340' side='right'caption='[[1kas]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1kas]] is a 1 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=1KAS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KAS 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]] 2.4&#8491;</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=1kas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kas OCA], [https://pdbe.org/1kas PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kas RCSB], [https://www.ebi.ac.uk/pdbsum/1kas PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kas ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABF_ECOLI FABF_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.
== 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/ka/1kas_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=1kas ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1KAS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]]. The following page contains interesting information on the relation of 1KAS with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb90_1.html Fatty Acid Synthase]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.41 2.3.1.41]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KAS OCA]].
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Crystal structure of beta-ketoacyl-acyl carrier protein synthase II from E.coli reveals the molecular architecture of condensing enzymes., Huang W, Jia J, Edwards P, Dehesh K, Schneider G, Lindqvist Y, EMBO J. 1998 Mar 2;17(5):1183-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9482715 9482715]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Fatty Acid Synthase]]
[[Category: Fatty Acid Synthase]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dehesh, K.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Edwards, P.]]
[[Category: Dehesh K]]
[[Category: Huang, W.]]
[[Category: Edwards P]]
[[Category: Jia, J.]]
[[Category: Huang W]]
[[Category: Lindqvist, Y.]]
[[Category: Jia J]]
[[Category: Schneider, G.]]
[[Category: Lindqvist Y]]
[[Category: acyltransferase]]
[[Category: Schneider G]]
[[Category: alpha-beta protein]]
[[Category: alpha-beta-alpha-beta-alpha]]
[[Category: condensing enzyme]]
[[Category: fatty acid elongation]]
[[Category: five-layered fold]]
[[Category: lipid metabolism]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 16:09:18 2007''

Latest revision as of 10:45, 7 February 2024

BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLIBETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI

Structural highlights

1kas is a 1 chain structure with sequence from Escherichia coli. The June 2007 RCSB PDB Molecule of the Month feature on Fatty Acid Synthase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABF_ECOLI Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis.

Evolutionary Conservation

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

See Also

1kas, resolution 2.40Å

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