1rla

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[[Image:1rla.gif|left|200px]]
[[Image:1rla.gif|left|200px]]
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{{Structure
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|PDB= 1rla |SIZE=350|CAPTION= <scene name='initialview01'>1rla</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1rla", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginase Arginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.1 3.5.3.1] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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{{STRUCTURE_1rla| PDB=1rla | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rla OCA], [http://www.ebi.ac.uk/pdbsum/1rla PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rla RCSB]</span>
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}}
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'''THREE-DIMENSIONAL STRUCTURE OF RAT LIVER ARGINASE, THE BINUCLEAR MANGANESE METALLOENZYME OF THE UREA CYCLE'''
'''THREE-DIMENSIONAL STRUCTURE OF RAT LIVER ARGINASE, THE BINUCLEAR MANGANESE METALLOENZYME OF THE UREA CYCLE'''
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[[Category: Kanyo, Z.]]
[[Category: Kanyo, Z.]]
[[Category: Scolnick, L.]]
[[Category: Scolnick, L.]]
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[[Category: arginine metabolism]]
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[[Category: Arginine metabolism]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: magnesium]]
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[[Category: Magnesium]]
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[[Category: urea cycle]]
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[[Category: Urea cycle]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:38:15 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:29:48 2008''
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Revision as of 04:38, 3 May 2008

Template:STRUCTURE 1rla

THREE-DIMENSIONAL STRUCTURE OF RAT LIVER ARGINASE, THE BINUCLEAR MANGANESE METALLOENZYME OF THE UREA CYCLE


Overview

Each individual excretes roughly 10 kg of urea per year, as a result of the hydrolysis of arginine in the final cytosolic step of the urea cycle. This reaction allows the disposal of nitrogenous waste from protein catabolism, and is catalysed by the liver arginase enzyme. In other tissues that lack a complete urea cycle, arginase regulates cellular arginine and ornithine concentrations for biosynthetic reactions, including nitric oxide synthesis: in the macrophage, arginase activity is reciprocally coordinated with that of NO synthase to modulate NO-dependent cytotoxicity. The bioinorganic chemistry of arginase is particularly rich because this enzyme is one of very few that specifically requires a spin-coupled Mn2+-Mn2+ cluster for catalytic activity in vitro and in vivo. The 2.1 angstrom-resolution crystal structure of trimeric rat liver arginase reveals that this unique metal cluster resides at the bottom of an active-site cleft that is 15 angstroms deep. Analysis of the structure indicates that arginine hydrolysis is achieved by a metal-activated solvent molecule which symmetrically bridges the two Mn2+ ions.

About this Structure

1RLA is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structure of a unique binuclear manganese cluster in arginase., Kanyo ZF, Scolnick LR, Ash DE, Christianson DW, Nature. 1996 Oct 10;383(6600):554-7. PMID:8849731 Page seeded by OCA on Sat May 3 07:38:15 2008

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