1nvj: Difference between revisions
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New page: left|200px<br /><applet load="1nvj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nvj, resolution 2.15Å" /> '''Deletion Mutant (Del... |
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[[Image:1nvj.gif|left|200px]]<br /><applet load="1nvj" size=" | [[Image:1nvj.gif|left|200px]]<br /><applet load="1nvj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nvj, resolution 2.15Å" /> | caption="1nvj, resolution 2.15Å" /> | ||
'''Deletion Mutant (Delta 141) of Molybdopterin Synthase'''<br /> | '''Deletion Mutant (Delta 141) of Molybdopterin Synthase'''<br /> | ||
==Overview== | ==Overview== | ||
Molybdenum cofactor biosynthesis is an evolutionarily conserved pathway | 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== | ==About this Structure== | ||
1NVJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with NA, GOL and FMT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1NVJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=FMT:'>FMT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NVJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Rajagopalan, K | [[Category: Rajagopalan, K V.]] | ||
[[Category: Rudolph, M | [[Category: Rudolph, M J.]] | ||
[[Category: Schindelin, H.]] | [[Category: Schindelin, H.]] | ||
[[Category: Turque, O.]] | [[Category: Turque, O.]] | ||
[[Category: Wuebbens, M | [[Category: Wuebbens, M M.]] | ||
[[Category: FMT]] | [[Category: FMT]] | ||
[[Category: GOL]] | [[Category: GOL]] | ||
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[[Category: molybdenum cofactor biosynthesis]] | [[Category: molybdenum cofactor biosynthesis]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:36 2008'' | ||
