7jdw: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:7jdw.jpg|left|200px]]
{{Seed}}
[[Image:7jdw.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_7jdw|  PDB=7jdw  |  SCENE=  }}  
{{STRUCTURE_7jdw|  PDB=7jdw  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH DELTA-AMINO VALERIC ACID'''
===CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH DELTA-AMINO VALERIC ACID===




==Overview==
<!--  
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.
The line below this paragraph, {{ABSTRACT_PUBMED_9915841}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 9915841 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_9915841}}


==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Novel fold]]
[[Category: Novel fold]]
[[Category: Reaction mechanism]]
[[Category: Reaction mechanism]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:46:26 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:40:36 2008''

Revision as of 11:40, 3 July 2008

File:7jdw.png

Template:STRUCTURE 7jdw

CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH DELTA-AMINO VALERIC ACID

Template:ABSTRACT PUBMED 9915841

About this Structure

7JDW is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Jul 3 14:40:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=7jdw&oldid=636344"