1r3w: Difference between revisions

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[[Image:1r3w.gif|left|200px]]<br /><applet load="1r3w" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1r3w.gif|left|200px]]
caption="1r3w, resolution 1.70&Aring;" />
 
'''Uroporphyrinogen Decarboxylase Y164F mutant in complex with coproporphyrinogen-III'''<br />
{{Structure
|PDB= 1r3w |SIZE=350|CAPTION= <scene name='initialview01'>1r3w</scene>, resolution 1.70&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CP3:COPROPORPHYRIN III'>CP3</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''Uroporphyrinogen Decarboxylase Y164F mutant in complex with coproporphyrinogen-III'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1R3W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CP3:'>CP3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R3W OCA].  
1R3W is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R3W OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14633982 14633982]
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:[http://www.ncbi.nlm.nih.gov/pubmed/14633982 14633982]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: uroporphyrinogen decarboxylase coproporphyrinogen; x-ray crystallography]]
[[Category: uroporphyrinogen decarboxylase coproporphyrinogen; x-ray crystallography]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:49 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:46:28 2008''

Revision as of 14:46, 20 March 2008

File:1r3w.gif


PDB ID 1r3w

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands:
Activity: Uroporphyrinogen decarboxylase, with EC number 4.1.1.37
Coordinates: save as pdb, mmCIF, xml



Uroporphyrinogen Decarboxylase Y164F mutant in complex with coproporphyrinogen-III


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.

DiseaseDisease

Known diseases associated with this structure: Porphyria cutanea tarda OMIM:[176100], Porphyria, hepatoerythropoietic OMIM:[176100]

About this StructureAbout this Structure

1R3W 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

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