1dd8: Difference between revisions

Revision as of 22:51, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1dd8.png

Template:STRUCTURE 1dd8

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

Template:ABSTRACT PUBMED 10571059

About this StructureAbout this Structure

1DD8 is a Single protein structure of sequence from Escherichia coli. 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

Page seeded by OCA on Mon Jun 30 22:51:13 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1dd8.gif|left|200px]]
+{{Seed}}
+[[Image:1dd8.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1dd8|  PDB=1dd8  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I FROM ESCHERICHIA COLI'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10571059}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10571059 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10571059}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Wettstein-Knowles, P von.]]
 [[Category: Thiolase fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:43:06 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:51:13 2008''