1fma
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(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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Revision as of 12:55, 20 November 2007
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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 CL 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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