1umf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1umf.gif|left|200px]]
[[Image:1umf.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1umf |SIZE=350|CAPTION= <scene name='initialview01'>1umf</scene>, resolution 2.25&Aring;
+
The line below this paragraph, containing "STRUCTURE_1umf", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chorismate_synthase Chorismate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.3.5 4.2.3.5] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1umf| PDB=1umf | SCENE= }}
-
|RELATEDENTRY=[[1um0|1UM0]]
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1umf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umf OCA], [http://www.ebi.ac.uk/pdbsum/1umf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1umf RCSB]</span>
+
-
}}
+
'''crystal structure of chorismate synthase'''
'''crystal structure of chorismate synthase'''
Line 30: Line 27:
[[Category: Suh, S W.]]
[[Category: Suh, S W.]]
[[Category: Yoon, H J.]]
[[Category: Yoon, H J.]]
-
[[Category: beta-alpha-beta sandwich fold]]
+
[[Category: Beta-alpha-beta sandwich fold]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:25:25 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:12:22 2008''
+

Revision as of 08:25, 3 May 2008

Image:1umf.gif

Template:STRUCTURE 1umf

crystal structure of chorismate synthase


Overview

Chorismate synthase catalyzes the conversion of 5-enolpyruvylshikimate 3-phosphate to chorismate in the shikimate pathway, which represents an attractive target for discovering antimicrobial agents and herbicides. Chorismate serves as a common precursor for the synthesis of aromatic amino acids and many aromatic compounds in microorganisms and plants. Chorismate synthase requires reduced FMN as a cofactor but the catalyzed reaction involves no net redox change. Here, we have determined the crystal structure of chorismate synthase from Helicobacter pylori in both FMN-bound and FMN-free forms. It is a tetrameric enzyme, with each monomer possessing a novel "beta-alpha-beta sandwich fold". Highly conserved regions, including several flexible loops, cluster together around the bound FMN to form the active site. The unique FMN-binding site is formed largely by a single subunit, with a small contribution from a neighboring subunit. The isoalloxazine ring of the bound FMN is significantly non-planar. Our structure illuminates the essential functional roles played by the cofactor.

About this Structure

1UMF is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.

Reference

Crystal structure of chorismate synthase: a novel FMN-binding protein fold and functional insights., Ahn HJ, Yoon HJ, Lee B 2nd, Suh SW, J Mol Biol. 2004 Feb 27;336(4):903-15. PMID:15095868 Page seeded by OCA on Sat May 3 11:25:25 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1umf"
Personal tools