1uro: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1uro.gif|left|200px]]
[[Image:1uro.gif|left|200px]]


{{Structure
<!--
|PDB= 1uro |SIZE=350|CAPTION= <scene name='initialview01'>1uro</scene>, resolution 1.80&Aring;
The line below this paragraph, containing "STRUCTURE_1uro", 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=BME:BETA-MERCAPTOETHANOL'>BME</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=  
-->
|DOMAIN=
{{STRUCTURE_1uro| PDB=1uro  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uro OCA], [http://www.ebi.ac.uk/pdbsum/1uro PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uro RCSB]</span>
}}


'''UROPORPHYRINOGEN DECARBOXYLASE'''
'''UROPORPHYRINOGEN DECARBOXYLASE'''
Line 30: Line 27:
[[Category: Phillips, J D.]]
[[Category: Phillips, J D.]]
[[Category: Whitby, F G.]]
[[Category: Whitby, F G.]]
[[Category: alpha-8-beta-8 barrel]]
[[Category: Alpha-8-beta-8 barrel]]
[[Category: decarboxylase]]
[[Category: Decarboxylase]]
[[Category: heme biosynthesis]]
[[Category: Heme biosynthesis]]
[[Category: porphyrin]]
[[Category: Porphyrin]]
[[Category: uroporphyrinogen]]
[[Category: Uroporphyrinogen]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 11:35:56 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:14:16 2008''

Revision as of 11:35, 3 May 2008

File:1uro.gif

Template:STRUCTURE 1uro

UROPORPHYRINOGEN DECARBOXYLASE


OverviewOverview

Uroporphyrinogen decarboxylase (URO-D) catalyzes the fifth step in the heme biosynthetic pathway, converting uroporphyrinogen to coproporphyrinogen by decarboxylating the four acetate side chains of the substrate. This activity is essential in all organisms, and subnormal activity of URO-D leads to the most common form of porphyria in humans, porphyria cutanea tarda (PCT). We have determined the crystal structure of recombinant human URO-D at 1.60 A resolution. The 40.8 kDa protein is comprised of a single domain containing a (beta/alpha)8-barrel with a deep active site cleft formed by loops at the C-terminal ends of the barrel strands. Many conserved residues cluster at this cleft, including the invariant side chains of Arg37, Arg41 and His339, which probably function in substrate binding, and Asp86, Tyr164 and Ser219, which may function in either binding or catalysis. URO-D is a dimer in solution (Kd = 0.1 microM), and this dimer also appears to be formed in the crystal. Assembly of the dimer juxtaposes the active site clefts of the monomers, suggesting a functionally important interaction between the catalytic centers.

About this StructureAbout this Structure

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

ReferenceReference

Crystal structure of human uroporphyrinogen decarboxylase., Whitby FG, Phillips JD, Kushner JP, Hill CP, EMBO J. 1998 May 1;17(9):2463-71. PMID:9564029 Page seeded by OCA on Sat May 3 11:35:56 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA