1b8g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1b8g.gif|left|200px]]
[[Image:1b8g.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1b8g |SIZE=350|CAPTION= <scene name='initialview01'>1b8g</scene>, resolution 2.37&Aring;
+
The line below this paragraph, containing "STRUCTURE_1b8g", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/1-aminocyclopropane-1-carboxylate_synthase 1-aminocyclopropane-1-carboxylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.14 4.4.1.14] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1b8g| PDB=1b8g | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b8g OCA], [http://www.ebi.ac.uk/pdbsum/1b8g PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b8g RCSB]</span>
+
-
}}
+
'''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE'''
'''1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE'''
Line 32: Line 29:
[[Category: Kirsch, J F.]]
[[Category: Kirsch, J F.]]
[[Category: Storici, P.]]
[[Category: Storici, P.]]
-
[[Category: ethylene biosynthesis]]
+
[[Category: Ethylene biosynthesis]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:12:15 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:55:43 2008''
+

Revision as of 08:12, 2 May 2008

Template:STRUCTURE 1b8g

1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE


Overview

The 2.4 A crystal structure of the vitamin B6-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase is described. This enzyme catalyses the committed step in the biosynthesis of ethylene, a plant hormone that is responsible for the initiation of fruit ripening and for regulating many other developmental processes. ACC synthase has 15 % sequence identity with the well-studied aspartate aminotransferase, and a completely different catalytic activity yet the overall folds and the active sites are very similar. The new structure together with available biochemical data enables a comparative mechanistic analysis that largely explains the catalytic roles of the conserved and non-conserved active site residues. An external aldimine reaction intermediate (external aldimine with ACC, i.e. with the product) has been modeled. The new structure provides a basis for the rational design of inhibitors with broad agricultural applications.

About this Structure

1B8G is a Single protein structure of sequence from Malus x domestica. Full crystallographic information is available from OCA.

Reference

Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene., Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN, J Mol Biol. 1999 Dec 3;294(3):745-56. PMID:10610793 Page seeded by OCA on Fri May 2 11:12:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools