1dd8
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == 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> | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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/main_output.php?pdb_ID=1dd8 ConSurf]. | </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> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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:10571059<ref>PMID:10571059</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1dd8" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | *[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Kadziola | + | [[Category: Kadziola A]] |
| - | [[Category: Larsen | + | [[Category: Larsen S]] |
| - | [[Category: Lindquist | + | [[Category: Lindquist Y]] |
| - | [[Category: Olsen | + | [[Category: Olsen JG]] |
| - | [[Category: Siggaard-Andersen | + | [[Category: Siggaard-Andersen M]] |
| - | [[Category: Wettstein-Knowles | + | [[Category: Von Wettstein-Knowles P]] |
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Current revision
CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI
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