1fma: Difference between revisions
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|PDB= 1fma |SIZE=350|CAPTION= <scene name='initialview01'>1fma</scene>, resolution 1.58Å | |PDB= 1fma |SIZE=350|CAPTION= <scene name='initialview01'>1fma</scene>, resolution 1.58Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1fmo|1FMO]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fma OCA], [http://www.ebi.ac.uk/pdbsum/1fma PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fma RCSB]</span> | |||
}} | }} | ||
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[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
[[Category: Wuebbens, M M.]] | [[Category: Wuebbens, M M.]] | ||
[[Category: isopeptide bond]] | [[Category: isopeptide bond]] | ||
[[Category: molybdenum cofactor biosynthesis]] | [[Category: molybdenum cofactor biosynthesis]] | ||
[[Category: transferase]] | [[Category: transferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:25:42 2008'' | ||
Revision as of 20:25, 30 March 2008
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| , resolution 1.58Å | |||||||
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| Ligands: | |||||||
| Related: | 1FMO
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)
OverviewOverview
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 StructureAbout this Structure
1FMA is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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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