1r3r: Difference between revisions

Revision as of 12:19, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1r3r.png

Template:STRUCTURE 1r3r

Uroporphyrinogen Decarboxylase with mutation D86NUroporphyrinogen Decarboxylase with mutation D86N

Template:ABSTRACT PUBMED 14633982

About this StructureAbout this Structure

1R3R 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 Tue Jul 29 12:19:31 2008

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OCA

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-[[Image:1r3r.gif|left|200px]]
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-'''Uroporphyrinogen Decarboxylase with mutation D86N'''
+===Uroporphyrinogen Decarboxylase with mutation D86N===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_14633982}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_14633982}}
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 [[Category: Uroporphyrinogen decarboxylase coproporphyrinogen]]
 [[Category: X-ray crystallography]]
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+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:19:31 2008''