1jdw: Difference between revisions

Revision as of 21:06, 2 May 2008

CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS

OverviewOverview

L-arginine:glycine amidinotransferase (AT) catalyses the committed step in creatine biosynthesis by formation of guanidinoacetic acid, the immediate precursor of creatine. We have determined the crystal structure of the recombinant human enzyme by multiple isomorphous replacement at 1.9 A resolution. A telluromethionine derivative was used in sequence assignment. The structure of AT reveals a new fold with 5-fold pseudosymmetry of circularly arranged betabeta alphabeta-modules. These enclose the active site compartment, which is accessible only through a narrow channel. The overall structure resembles a basket with handles that are formed from insertions into the betabeta alphabeta-modules. Binding of L-ornithine, a product inhibitor, reveals a marked induced-fit mechanism, with a loop at the active site entrance changing its conformation accompanied by a shift of an alpha-helix by -4 A. Binding of the arginine educt to the inactive mutant C407A shows a similar mode of binding. A reaction mechanism with a catalytic triad Cys-His-Asp is proposed on the basis of substrate and product bound states.

About this StructureAbout this Structure

1JDW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis., Humm A, Fritsche E, Steinbacher S, Huber R, EMBO J. 1997 Jun 16;16(12):3373-85. PMID:9218780 Page seeded by OCA on Fri May 2 21:06:22 2008

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OCA

@@ Line 1: / Line 1: @@
 [[Image:1jdw.gif|left|200px]]
- {{Structure
+<!--
-|PDB= 1jdw |SIZE=350|CAPTION= <scene name='initialview01'>1jdw</scene>, resolution 1.90&Aring;
+The line below this paragraph, containing "STRUCTURE_1jdw", 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=BME:BETA-MERCAPTOETHANOL'>BME</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/Glycine_amidinotransferase Glycine amidinotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.4.1 2.1.4.1] </span>
+or leave the SCENE parameter empty for the default display.
-|GENE= AT38H ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
+-->
-|DOMAIN=
+{{STRUCTURE_1jdw|  PDB=1jdw  |  SCENE=  }}
-|RELATEDENTRY=
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdw OCA], [http://www.ebi.ac.uk/pdbsum/1jdw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jdw RCSB]</span>
-}}
 '''CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS'''
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 [[Category: Humm, A.]]
 [[Category: Steinbacher, S.]]
-[[Category: catalytic triad]]
+[[Category: Catalytic triad]]
-[[Category: creatine biosynthesis]]
+[[Category: Creatine biosynthesis]]
-[[Category: fivefold pseudosymmetry]]
+[[Category: Fivefold pseudosymmetry]]
-[[Category: novel fold]]
+[[Category: Novel fold]]
-[[Category: reaction mechanism]]
+[[Category: Reaction mechanism]]
-[[Category: transferase]]
+[[Category: Transferase]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:06:22 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:14 2008''