1dd8: Difference between revisions

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New page: left|200px<br /><applet load="1dd8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dd8, resolution 2.3Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1dd8.gif|left|200px]]<br /><applet load="1dd8" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1dd8, resolution 2.3&Aring;" />
'''CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI'''<br />


==Overview==
==CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI==
The crystal structure of the fatty acid elongating enzyme beta-ketoacyl, [acyl carrier protein] synthase I (KAS I) from Escherichia coli has been, determined to 2.3 A resolution by molecular replacement using the recently, solved crystal structure of KAS II as a search model. The crystal contains, two independent dimers in the asymmetric unit. KAS I assumes the thiolase, alpha(beta)alpha(beta)alpha fold. Electrostatic potential distribution, reveals an acyl carrier protein docking site and a presumed substrate, binding pocket was detected extending the active site. Both subunits, contribute to each substrate binding site in the dimer.
<StructureSection load='1dd8' size='340' side='right'caption='[[1dd8]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1dd8]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DD8 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]] 2.3&#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=1dd8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dd8 OCA], [https://pdbe.org/1dd8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dd8 RCSB], [https://www.ebi.ac.uk/pdbsum/1dd8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dd8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABB_ECOLI FABB_ECOLI] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids.
== 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/dd/1dd8_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=1dd8 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1DD8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Beta-ketoacyl-acyl-carrier-protein_synthase_I Beta-ketoacyl-acyl-carrier-protein synthase I], 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=1DD8 OCA].
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The X-ray crystal structure of beta-ketoacyl [acyl carrier protein] synthase I., Olsen JG, Kadziola A, von Wettstein-Knowles P, Siggaard-Andersen M, Lindquist Y, Larsen S, FEBS Lett. 1999 Oct 22;460(1):46-52. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10571059 10571059]
[[Category: Beta-ketoacyl-acyl-carrier-protein synthase I]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Kadziola, A.]]
[[Category: Kadziola A]]
[[Category: Larsen, S.]]
[[Category: Larsen S]]
[[Category: Lindquist, Y.]]
[[Category: Lindquist Y]]
[[Category: Olsen, J.G.]]
[[Category: Olsen JG]]
[[Category: Siggaard-Andersen, M.]]
[[Category: Siggaard-Andersen M]]
[[Category: Wettstein-Knowles, P.von.]]
[[Category: Von Wettstein-Knowles P]]
[[Category: thiolase fold]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:11:22 2007''

Latest revision as of 09:52, 7 February 2024

CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLICRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI

Structural highlights

1dd8 is a 4 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABB_ECOLI Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids.

Evolutionary Conservation

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

See Also

1dd8, resolution 2.30Å

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