1fma: Difference between revisions

Revision as of 03:28, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1fma.png

Template:STRUCTURE 1fma

MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)

Template:ABSTRACT PUBMED 11135669

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

Page seeded by OCA on Tue Jul 1 03:28:39 2008

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

OCA

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-[[Image:1fma.gif|left|200px]]
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-'''MOLYBDOPTERIN SYNTHASE (MOAD/MOAE)'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11135669}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_11135669}}
 ==About this Structure==
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 [[Category: Molybdenum cofactor biosynthesis]]
 [[Category: Transferase]]
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