1saw
From Proteopedia
(New page: 200px<br /> <applet load="1saw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1saw, resolution 2.20Å" /> '''X-ray structure of ...) |
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| - | [[Image:1saw.gif|left|200px]]<br /> | + | [[Image:1saw.gif|left|200px]]<br /><applet load="1saw" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1saw" size=" | + | |
caption="1saw, resolution 2.20Å" /> | caption="1saw, resolution 2.20Å" /> | ||
'''X-ray structure of homo sapiens protein FLJ36880'''<br /> | '''X-ray structure of homo sapiens protein FLJ36880'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The human protein FLJ36880 belongs to the fumarylacetoacetate hydrolase | + | The human protein FLJ36880 belongs to the fumarylacetoacetate hydrolase family. The X-ray structure of FLJ36880 has been determined to 2.2 A resolution employing the semi-automated high-throughput structural genomics approach of the Protein Structure Factory. FLJ36880 adopts a mixed beta-sandwich roll fold and forms homodimers in crystals as well as in solution. One Mg2+ ion is bound to each subunit of the dimeric protein by coordination to three carboxylate oxygens and three water molecules. These metal binding sites are accessible from the same surface of the dimer, partly due to the disorder of the undecapeptide stretch D29 to L39. The overall structure and metal binding site of FLJ36880 bear clear similarities to the C-terminal domain of the bifunctional enzyme HpcE from Escherichia coli C, fumarylacetoacetate hydrolase from Mus musculus and to YcgM (Apc5008) from E. coli 1262. These similarities provide a framework for suggesting biochemical functions and evolutionary relationships of FLJ36880. It appears highly probable that the metal binding sites are involved in an enzymatic activity related to the catabolism of aromatic amino acids. Two point mutations in the active-site of FAH, responsible for the metabolic disease hereditary tyrosinemia type I (HTI) in humans, affect residues that are structurally conserved in FLJ36880 and located in the putative catalytic site. |
==About this Structure== | ==About this Structure== | ||
| - | 1SAW 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 MG and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SAW 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=MG:'>MG</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Goetz, F.]] | [[Category: Goetz, F.]] | ||
[[Category: Heinemann, U.]] | [[Category: Heinemann, U.]] | ||
| - | [[Category: Manjasetty, B | + | [[Category: Manjasetty, B A.]] |
| - | [[Category: Niesen, F | + | [[Category: Niesen, F H.]] |
[[Category: Sievert, V.]] | [[Category: Sievert, V.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:40 2008'' |
Revision as of 12:59, 21 February 2008
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X-ray structure of homo sapiens protein FLJ36880
Overview
The human protein FLJ36880 belongs to the fumarylacetoacetate hydrolase family. The X-ray structure of FLJ36880 has been determined to 2.2 A resolution employing the semi-automated high-throughput structural genomics approach of the Protein Structure Factory. FLJ36880 adopts a mixed beta-sandwich roll fold and forms homodimers in crystals as well as in solution. One Mg2+ ion is bound to each subunit of the dimeric protein by coordination to three carboxylate oxygens and three water molecules. These metal binding sites are accessible from the same surface of the dimer, partly due to the disorder of the undecapeptide stretch D29 to L39. The overall structure and metal binding site of FLJ36880 bear clear similarities to the C-terminal domain of the bifunctional enzyme HpcE from Escherichia coli C, fumarylacetoacetate hydrolase from Mus musculus and to YcgM (Apc5008) from E. coli 1262. These similarities provide a framework for suggesting biochemical functions and evolutionary relationships of FLJ36880. It appears highly probable that the metal binding sites are involved in an enzymatic activity related to the catabolism of aromatic amino acids. Two point mutations in the active-site of FAH, responsible for the metabolic disease hereditary tyrosinemia type I (HTI) in humans, affect residues that are structurally conserved in FLJ36880 and located in the putative catalytic site.
About this Structure
1SAW is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
X-ray structure of fumarylacetoacetate hydrolase family member Homo sapiens FLJ36880., Manjasetty BA, Niesen FH, Delbruck H, Gotz F, Sievert V, Bussow K, Behlke J, Heinemann U, Biol Chem. 2004 Oct;385(10):935-42. PMID:15551868
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