1p90
From Proteopedia
(New page: 200px<br /><applet load="1p90" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p90, resolution 1.8Å" /> '''The Three-dimensional...) |
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| - | [[Image:1p90.jpg|left|200px]]<br /><applet load="1p90" size=" | + | [[Image:1p90.jpg|left|200px]]<br /><applet load="1p90" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1p90, resolution 1.8Å" /> | caption="1p90, resolution 1.8Å" /> | ||
'''The Three-dimensional Structure of the Core Domain of NafY from Azotobacter vinelandii determined at 1.8 resolution'''<br /> | '''The Three-dimensional Structure of the Core Domain of NafY from Azotobacter vinelandii determined at 1.8 resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Azotobacter vinelandii NafY protein (nitrogenase accessory factor Y) | + | The Azotobacter vinelandii NafY protein (nitrogenase accessory factor Y) is able to bind either to the iron molybdenum cofactor (FeMo-co) or to apodinitrogenase and is believed to facilitate the transfer of FeMo-co into apodinitrogenase. The NafY protein has two domains: an N-terminal domain (residues Met1-Leu98) and a C-terminal domain (residues Glu99-Ser232), referred here to as the "core domain." The core domain of NafY is shown here to be capable of binding the FeMo cofactor of nitrogenase but unable to bind to apodinitrogenase in the absence of the first domain. The three-dimensional molecular structure of the core domain of NafY has been solved to 1.8-A resolution, revealing that the protein consists of a mixed five-stranded beta-sheet flanked by five alpha-helices that belongs to the ribonuclease H superfamily. As such, this represents a new fold capable of binding FeMo-co, where the only previous example was that seen in dinitrogenase. |
==About this Structure== | ==About this Structure== | ||
| - | 1P90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with EDO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1P90 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii] with <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P90 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Azotobacter vinelandii]] | [[Category: Azotobacter vinelandii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dyer, D | + | [[Category: Dyer, D H.]] |
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
| - | [[Category: Ludden, P | + | [[Category: Ludden, P W.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: Rubio, L | + | [[Category: Rubio, L M.]] |
| - | [[Category: Thoden, J | + | [[Category: Thoden, J B.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: ribonuclease h motif]] | [[Category: ribonuclease h motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:26:26 2008'' |
Revision as of 12:26, 21 February 2008
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The Three-dimensional Structure of the Core Domain of NafY from Azotobacter vinelandii determined at 1.8 resolution
Overview
The Azotobacter vinelandii NafY protein (nitrogenase accessory factor Y) is able to bind either to the iron molybdenum cofactor (FeMo-co) or to apodinitrogenase and is believed to facilitate the transfer of FeMo-co into apodinitrogenase. The NafY protein has two domains: an N-terminal domain (residues Met1-Leu98) and a C-terminal domain (residues Glu99-Ser232), referred here to as the "core domain." The core domain of NafY is shown here to be capable of binding the FeMo cofactor of nitrogenase but unable to bind to apodinitrogenase in the absence of the first domain. The three-dimensional molecular structure of the core domain of NafY has been solved to 1.8-A resolution, revealing that the protein consists of a mixed five-stranded beta-sheet flanked by five alpha-helices that belongs to the ribonuclease H superfamily. As such, this represents a new fold capable of binding FeMo-co, where the only previous example was that seen in dinitrogenase.
About this Structure
1P90 is a Single protein structure of sequence from Azotobacter vinelandii with as ligand. Full crystallographic information is available from OCA.
Reference
The three-dimensional structure of the core domain of Naf Y from Azotobacter vinelandii determined at 1.8-A resolution., Dyer DH, Rubio LM, Thoden JB, Holden HM, Ludden PW, Rayment I, J Biol Chem. 2003 Aug 22;278(34):32150-6. Epub 2003 May 16. PMID:12754195
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