1yni

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|PDB= 1yni |SIZE=350|CAPTION= <scene name='initialview01'>1yni</scene>, resolution 2.20&Aring;
|PDB= 1yni |SIZE=350|CAPTION= <scene name='initialview01'>1yni</scene>, resolution 2.20&Aring;
|SITE=
|SITE=
-
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=SUG:N~2~-(3-CARBOXYPROPANOYL)-L-ARGININE'>SUG</scene>
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|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SUG:N~2~-(3-CARBOXYPROPANOYL)-L-ARGININE'>SUG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=[[1ynf|1YNF]], [[1ynh|1YNH]]
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1yni FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yni OCA], [http://www.ebi.ac.uk/pdbsum/1yni PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1yni RCSB]</span>
}}
}}
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[[Category: Schrag, J D.]]
[[Category: Schrag, J D.]]
[[Category: Tocilj, A.]]
[[Category: Tocilj, A.]]
-
[[Category: K]]
 
-
[[Category: SUG]]
 
[[Category: bsgi]]
[[Category: bsgi]]
[[Category: dihydrolase]]
[[Category: dihydrolase]]
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[[Category: succinylarginine]]
[[Category: succinylarginine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:25:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:14:57 2008''

Revision as of 22:15, 30 March 2008

Image:1yni.gif


PDB ID 1yni

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: ,
Related: 1YNF, 1YNH


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of N-Succinylarginine Dihydrolase, AstB, bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli


Overview

The ammonia-producing arginine succinyltransferase pathway is the major pathway in Escherichia coli and related bacteria for arginine catabolism as a sole nitrogen source. This pathway consists of five steps, each catalyzed by a distinct enzyme. Here we report the crystal structure of N-succinylarginine dihydrolase AstB, the second enzyme of the arginine succinyltransferase pathway, providing the first structural insight into enzymes from this pathway. The enzyme exhibits a pseudo 5-fold symmetric alpha/beta propeller fold of circularly arranged betabetaalphabeta modules enclosing the active site. The crystal structure indicates clearly that this enzyme belongs to the amidinotransferase (AT) superfamily and that the active site contains a Cys-His-Glu triad characteristic of the AT superfamily. Structures of the complexes of AstB with the reaction product and a C365S mutant with bound the N-succinylarginine substrate suggest a catalytic mechanism that consists of two cycles of hydrolysis and ammonia release, with each cycle utilizing a mechanism similar to that proposed for arginine deiminases. Like other members of the AT superfamily of enzymes, AstB possesses a flexible loop that is disordered in the absence of substrate and assumes an ordered conformation upon substrate binding, shielding the ligand from the bulk solvent, thereby controlling substrate access and product release.

About this Structure

1YNI is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of N-succinylarginine dihydrolase AstB, bound to substrate and product, an enzyme from the arginine catabolic pathway of Escherichia coli., Tocilj A, Schrag JD, Li Y, Schneider BL, Reitzer L, Matte A, Cygler M, J Biol Chem. 2005 Apr 22;280(16):15800-8. Epub 2005 Feb 9. PMID:15703173

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