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3jdw
From Proteopedia
| 3jdw, resolution 2.40Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Ligands: | |||||||||
| Gene: | AT38H (Homo sapiens) | ||||||||
| Activity: | Glycine amidinotransferase, with EC number 2.1.4.1 | ||||||||
| Domains: | Amidinotransf, COG1834 | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3JDW is a 1 chain structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Humm A, Fritsche E, Steinbacher S, Huber R. Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. EMBO J. 1997 Jun 16;16(12):3373-85. PMID:9218780 doi:10.1093/emboj/16.12.3373
Page seeded by OCA on Wed Feb 18 08:47:39 2009
