1nvj
From Proteopedia
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| - | [[Image:1nvj.gif|left|200px]] | + | [[Image:1nvj.gif|left|200px]] |
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| - | '''Deletion Mutant (Delta 141) of Molybdopterin Synthase''' | + | {{Structure |
| + | |PDB= 1nvj |SIZE=350|CAPTION= <scene name='initialview01'>1nvj</scene>, resolution 2.15Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> and <scene name='pdbligand=FMT:FORMIC ACID'>FMT</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= MOAE OR CHLA5 OR B0785 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Deletion Mutant (Delta 141) of Molybdopterin Synthase''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NVJ is a [ | + | 1NVJ 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=1NVJ OCA]. |
==Reference== | ==Reference== | ||
| - | Structural studies of molybdopterin synthase provide insights into its catalytic mechanism., Rudolph MJ, Wuebbens MM, Turque O, Rajagopalan KV, Schindelin H, J Biol Chem. 2003 Apr 18;278(16):14514-22. Epub 2003 Feb 5. PMID:[http:// | + | Structural studies of molybdopterin synthase provide insights into its catalytic mechanism., Rudolph MJ, Wuebbens MM, Turque O, Rajagopalan KV, Schindelin H, J Biol Chem. 2003 Apr 18;278(16):14514-22. Epub 2003 Feb 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12571227 12571227] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: molybdenum cofactor biosynthesis]] | [[Category: molybdenum cofactor biosynthesis]] | ||
| - | ''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 13:02:13 2008'' |
Revision as of 11:02, 20 March 2008
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| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | MOAE OR CHLA5 OR B0785 (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Deletion Mutant (Delta 141) of Molybdopterin Synthase
Overview
Molybdenum cofactor biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes, including humans. Genetic deficiencies of enzymes involved in cofactor biosynthesis in humans lead to a severe and usually fatal disease. The molybdenum cofactor contains a tricyclic pyranopterin, termed molybdopterin, that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of molybdopterin is generated by molybdopterin synthase, which consists of a large (MoaE) and small (MoaD) subunit. The crystal structure of molybdopterin synthase revealed a heterotetrameric enzyme in which the C terminus of each MoaD subunit is deeply inserted into a MoaE subunit to form the active site. In the activated form of the enzyme, the MoaD C terminus is present as a thiocarboxylate. The present study identified the position of the thiocarboxylate sulfur by exploiting the anomalous signal originating from the sulfur atom. The structure of molybdopterin synthase in a novel crystal form revealed a binding pocket for the terminal phosphate of molybdopterin, the product of the enzyme, and suggested a binding site for the pterin moiety present in precursor Z and molybdopterin. Finally, the crystal structure of the MoaE homodimer provides insights into the conformational changes accompanying binding of the MoaD subunit.
About this Structure
1NVJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural studies of molybdopterin synthase provide insights into its catalytic mechanism., Rudolph MJ, Wuebbens MM, Turque O, Rajagopalan KV, Schindelin H, J Biol Chem. 2003 Apr 18;278(16):14514-22. Epub 2003 Feb 5. PMID:12571227
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