1dd8
From Proteopedia
(New page: 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=" | + | [[Image:1dd8.gif|left|200px]]<br /><applet load="1dd8" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dd8, resolution 2.3Å" /> | caption="1dd8, resolution 2.3Å" /> | ||
'''CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI'''<br /> | '''CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the fatty acid elongating enzyme beta-ketoacyl | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1DD8 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Larsen, S.]] | [[Category: Larsen, S.]] | ||
[[Category: Lindquist, Y.]] | [[Category: Lindquist, Y.]] | ||
| - | [[Category: Olsen, J | + | [[Category: Olsen, J G.]] |
[[Category: Siggaard-Andersen, M.]] | [[Category: Siggaard-Andersen, M.]] | ||
| - | [[Category: Wettstein-Knowles, P | + | [[Category: Wettstein-Knowles, P von.]] |
[[Category: thiolase fold]] | [[Category: thiolase fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:26 2008'' |
Revision as of 10:15, 21 February 2008
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CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI
Overview
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.
About this Structure
1DD8 is a Single protein structure of sequence from Escherichia coli. Active as Beta-ketoacyl-acyl-carrier-protein synthase I, with EC number 2.3.1.41 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:15:26 2008
