1fma
From Proteopedia
(New page: 200px<br /><applet load="1fma" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fma, resolution 1.58Å" /> '''MOLYBDOPTERIN SYNTHA...) |
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| - | [[Image:1fma.gif|left|200px]]<br /><applet load="1fma" size=" | + | [[Image:1fma.gif|left|200px]]<br /><applet load="1fma" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fma, resolution 1.58Å" /> | caption="1fma, resolution 1.58Å" /> | ||
'''MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)'''<br /> | '''MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved | + | Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes, including humans. Genetic deficiencies of enzymes involved in Moco biosynthesis in humans lead to a severe and usually fatal disease. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of MPT is generated by MPT synthase, which consists of a large and small subunits. The 1.45 A resolution crystal structure of MPT synthase reveals a heterotetrameric protein in which the C-terminus of each small subunit is inserted into a large subunit to form the active site. In the activated form of the enzyme this C-terminus is present as a thiocarboxylate. In the structure of a covalent complex of MPT synthase, an isopeptide bond is present between the C-terminus of the small subunit and a Lys side chain in the large subunit. The strong structural similarity between the small subunit of MPT synthase and ubiquitin provides evidence for the evolutionary antecedence of the Moco biosynthetic pathway to the ubiquitin dependent protein degradation pathway. |
==About this Structure== | ==About this Structure== | ||
| - | 1FMA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1FMA is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FMA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Rajagolpalan, K | + | [[Category: Rajagolpalan, K V.]] |
| - | [[Category: Rudolph, M | + | [[Category: Rudolph, M J.]] |
[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
| - | [[Category: Wuebbens, M | + | [[Category: Wuebbens, M M.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: isopeptide bond]] | [[Category: isopeptide bond]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:08 2008'' |
Revision as of 10:40, 21 February 2008
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MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)
Overview
Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes, including humans. Genetic deficiencies of enzymes involved in Moco biosynthesis in humans lead to a severe and usually fatal disease. Moco contains a tricyclic pyranopterin, termed molybdopterin (MPT), that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of MPT is generated by MPT synthase, which consists of a large and small subunits. The 1.45 A resolution crystal structure of MPT synthase reveals a heterotetrameric protein in which the C-terminus of each small subunit is inserted into a large subunit to form the active site. In the activated form of the enzyme this C-terminus is present as a thiocarboxylate. In the structure of a covalent complex of MPT synthase, an isopeptide bond is present between the C-terminus of the small subunit and a Lys side chain in the large subunit. The strong structural similarity between the small subunit of MPT synthase and ubiquitin provides evidence for the evolutionary antecedence of the Moco biosynthetic pathway to the ubiquitin dependent protein degradation pathway.
About this Structure
1FMA is a Protein complex structure of sequences from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation., Rudolph MJ, Wuebbens MM, Rajagopalan KV, Schindelin H, Nat Struct Biol. 2001 Jan;8(1):42-6. PMID:11135669
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