1di6
From Proteopedia
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| - | [[Image:1di6.gif|left|200px]] | + | [[Image:1di6.gif|left|200px]] |
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| - | '''1.45 A CRYSTAL STRUCTURE OF THE MOLYBDENUMM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI''' | + | {{Structure |
| + | |PDB= 1di6 |SIZE=350|CAPTION= <scene name='initialview01'>1di6</scene>, resolution 1.45Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''1.45 A CRYSTAL STRUCTURE OF THE MOLYBDENUMM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DI6 is a [ | + | 1DI6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DI6 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli., Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H, J Biol Chem. 2000 Jan 21;275(3):1814-22. PMID:[http:// | + | Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli., Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H, J Biol Chem. 2000 Jan 21;275(3):1814-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10636880 10636880] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: molybdenum cofactor]] | [[Category: molybdenum cofactor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:38:44 2008'' |
Revision as of 08:38, 20 March 2008
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| , resolution 1.45Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
1.45 A CRYSTAL STRUCTURE OF THE MOLYBDENUMM COFACTOR BIOSYNTHESIS PROTEIN MOGA FROM ESCHERICHIA COLI
Overview
Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway in archaea, eubacteria, and eukaryotes, including humans. Genetic deficiencies of enzymes involved in this biosynthetic pathway trigger an autosomal recessive disease with severe neurological symptoms, which usually leads to death in early childhood. The MogA protein exhibits affinity for molybdopterin, the organic component of Moco, and has been proposed to act as a molybdochelatase incorporating molybdenum into Moco. MogA is related to the protein gephyrin, which, in addition to its role in Moco biosynthesis, is also responsible for anchoring glycinergic receptors to the cytoskeleton at inhibitory synapses. The high resolution crystal structure of the Escherichia coli MogA protein has been determined, and it reveals a trimeric arrangement in which each monomer contains a central, mostly parallel beta-sheet surrounded by alpha-helices on either side. Based on structural and biochemical data, a putative active site was identified, including two residues that are essential for the catalytic mechanism.
About this Structure
1DI6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli., Liu MT, Wuebbens MM, Rajagopalan KV, Schindelin H, J Biol Chem. 2000 Jan 21;275(3):1814-22. PMID:10636880
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