1jdx: Difference between revisions
New page: left|200px<br /> <applet load="1jdx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdx, resolution 2.4Å" /> '''CRYSTAL STRUCTURE OF... |
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'''CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH L-NORVALINE'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH L-NORVALINE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1JDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NVA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1JDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NVA:'>NVA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDX OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: reaction mechanism]] | [[Category: reaction mechanism]] | ||
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Revision as of 17:06, 15 February 2008
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CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH L-NORVALINE
OverviewOverview
Human L-arginine:glycine amidinotransferase (AT) shows large structural, changes of the 300-flap and of helix H9 upon binding of L-arginine and, L-ornithine, described as a closed and an open conformation (Humm, A., Fritsche, E., Steinbacher, S., and Huber, R. (1997) EMBO J. 16, 3373-3385). To elucidate the structural basis of these induced-fit, movements, the x-ray structures of AT in complex with the amidino acceptor, glycine and its analogs gamma-aminobutyric acid and delta-aminovaleric, acid, as well as in complex with the amidino donor analogs L-alanine, L-alpha-aminobutyric acid, and L-norvaline, have been solved at 2.6-, 2.5-, 2.37-, 2.3-, 2.5-, and 2.4-A resolutions, respectively. The latter, three compounds were found to stabilize the open conformer. The glycine, analogs bind in a distinct manner and do not induce the transition to the, open state. The complex with glycine revealed a third binding mode, reflecting the rather broad substrate specificity of AT. These findings, identified a role for the alpha-amino group of the ligand in stabilizing, the open conformer. The kinetic, structural, and thermodynamic properties, of the mutants ATDeltaM302 and ATDelta11 (lacks 11 residues of H9), confirmed the key role of Asn300 and suggest that in mammalian, amidinotransferases, the role of helix H9 is in accelerating amidino, transfer by an induced-fit mechanism. Helix H9 does not add to the, stability of the protein.
DiseaseDisease
Known diseases associated with this structure: AGAT deficiency OMIM:[602360]
About this StructureAbout this Structure
1JDX is a Single protein structure of sequence from Homo sapiens with as ligand. Active as Glycine amidinotransferase, with EC number 2.1.4.1 Full crystallographic information is available from OCA.
ReferenceReference
The ligand-induced structural changes of human L-Arginine:Glycine amidinotransferase. A mutational and crystallographic study., Fritsche E, Humm A, Huber R, J Biol Chem. 1999 Jan 29;274(5):3026-32. PMID:9915841
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