4jdw
From Proteopedia
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| - | [[Image:4jdw.jpg|left|200px]] | + | [[Image:4jdw.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS''' | + | {{Structure |
| + | |PDB= 4jdw |SIZE=350|CAPTION= <scene name='initialview01'>4jdw</scene>, resolution 2.50Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ARG:ARGININE'>ARG</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= AT38H ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 4JDW is a [ | + | 4JDW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JDW OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9218780 9218780] |
[[Category: Glycine amidinotransferase]] | [[Category: Glycine amidinotransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:10:04 2008'' |
Revision as of 17:10, 20 March 2008
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| , resolution 2.50Å | |||||||
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| Ligands: | |||||||
| Gene: | AT38H (Homo sapiens) | ||||||
| Activity: | Glycine amidinotransferase, with EC number 2.1.4.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS
Contents |
Overview
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.
Disease
Known diseases associated with this structure: AGAT deficiency OMIM:[602360]
About this Structure
4JDW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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