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"  
[[Image:1dd8.gif|left|200px]]<br /><applet load="1dd8" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dd8, resolution 2.3&Aring;" />
caption="1dd8, resolution 2.3&Aring;" />
'''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, [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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DD8 OCA].  
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.G.]]
[[Category: Olsen, J G.]]
[[Category: Siggaard-Andersen, M.]]
[[Category: Siggaard-Andersen, M.]]
[[Category: Wettstein-Knowles, P.von.]]
[[Category: Wettstein-Knowles, P von.]]
[[Category: thiolase fold]]
[[Category: thiolase fold]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:11:22 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:15:26 2008''

Revision as of 13:15, 21 February 2008

File:1dd8.gif


1dd8, resolution 2.3Å

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

OverviewOverview

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 StructureAbout 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.

ReferenceReference

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

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