1r3q: Difference between revisions

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[[Image:1r3q.gif|left|200px]]
[[Image:1r3q.gif|left|200px]]


{{Structure
<!--
|PDB= 1r3q |SIZE=350|CAPTION= <scene name='initialview01'>1r3q</scene>, resolution 1.70&Aring;
The line below this paragraph, containing "STRUCTURE_1r3q", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=1CP:COPROPORPHYRIN+I'>1CP</scene>, <scene name='pdbligand=CO2:CARBON+DIOXIDE'>CO2</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Uroporphyrinogen_decarboxylase Uroporphyrinogen decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.37 4.1.1.37] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
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|DOMAIN=
{{STRUCTURE_1r3q| PDB=1r3q  | SCENE= }}  
|RELATEDENTRY=[[1uro|1URO]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r3q OCA], [http://www.ebi.ac.uk/pdbsum/1r3q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r3q RCSB]</span>
}}


'''Uroporphyrinogen Decarboxylase in complex with coproporphyrinogen-I'''
'''Uroporphyrinogen Decarboxylase in complex with coproporphyrinogen-I'''
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[[Category: Phillips, J D.]]
[[Category: Phillips, J D.]]
[[Category: Whitby, F G.]]
[[Category: Whitby, F G.]]
[[Category: uroporphyrinogen decarboxylase coproporphyrinogen]]
[[Category: Uroporphyrinogen decarboxylase coproporphyrinogen]]
[[Category: x-ray crystallography]]
[[Category: X-ray crystallography]]
 
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Revision as of 07:02, 3 May 2008

File:1r3q.gif

Template:STRUCTURE 1r3q

Uroporphyrinogen Decarboxylase in complex with coproporphyrinogen-I


OverviewOverview

Uroporphyrinogen decarboxylase (URO-D), an essential enzyme that functions in the heme biosynthetic pathway, catalyzes decarboxylation of all four acetate groups of uroporphyrinogen to form coproporphyrinogen. Here we report crystal structures of URO-D in complex with the I and III isomer coproporphyrinogen products. Crystallization required use of a novel enzymatic approach to generate the highly oxygen-sensitive porphyrinogen substrate in situ. The tetrapyrrole product adopts a domed conformation that lies against a collar of conserved hydrophobic residues and allows formation of hydrogen bonding interactions between a carboxylate oxygen atom of the invariant Asp86 residue and the pyrrole NH groups. Structural and biochemical analyses of URO-D proteins mutated at Asp86 support the conclusion that this residue makes important contributions to binding and likely promotes catalysis by stabilizing a positive charge on a reaction intermediate. The central coordination geometry of Asp86 allows the initial substrates and the various partially decarboxylated intermediates to be bound with equivalent activating interactions, and thereby explains how all four of the substrate acetate groups can be decarboxylated at the same catalytic center.

About this StructureAbout this Structure

1R3Q is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for tetrapyrrole coordination by uroporphyrinogen decarboxylase., Phillips JD, Whitby FG, Kushner JP, Hill CP, EMBO J. 2003 Dec 1;22(23):6225-33. PMID:14633982 Page seeded by OCA on Sat May 3 07:02:17 2008

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