1mio
From Proteopedia
(New page: 200px<br /><applet load="1mio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mio, resolution 3.0Å" /> '''X-RAY CRYSTAL STRUCTU...) |
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| - | [[Image:1mio.gif|left|200px]]<br /><applet load="1mio" size=" | + | [[Image:1mio.gif|left|200px]]<br /><applet load="1mio" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1mio, resolution 3.0Å" /> | caption="1mio, resolution 3.0Å" /> | ||
'''X-RAY CRYSTAL STRUCTURE OF THE NITROGENASE MOLYBDENUM-IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM AT 3.0 ANGSTROMS RESOLUTION'''<br /> | '''X-RAY CRYSTAL STRUCTURE OF THE NITROGENASE MOLYBDENUM-IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM AT 3.0 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the nitrogenase molybdenum-iron (MoFe) protein | + | The crystal structure of the nitrogenase molybdenum-iron (MoFe) protein from Clostridium pasteurianum (Cp1) has been determined at 3.0-A resolution by a combination of isomorphous replacement, molecular replacement, and noncrystallographic symmetry averaging. The structure of Cp1, including the two types of metal centers associated with the protein (the FeMo-cofactor and the P-cluster pair), is similar to that previously described for the MoFe-protein from Azotobacter vinelandii (Av1). Unique features of the Cp1 structure arise from the presence of an approximately 50-residue insertion in the alpha subunit and an approximately 50-residue deletion in the beta subunit. As a consequence, the FeMo-cofactor is more buried in Cp1 than in Av1, since the insertion is located on the surface above the FeMo-cofactor. The location of this insertion near the putative nitrogenase iron protein binding site provides a structural basis for the observation that the nitrogenase proteins from C. pasteurianum have low activity with complementary nitrogenase proteins isolated from other organisms. Mechanistic implications of the Cp1 structure for substrate entry/product release, substrate binding to the FeMo-cofactor, and electron- and proton-transfer reactions of nitrogenase are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1MIO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum] with CA, HCA, CFM and CLP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1MIO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_pasteurianum Clostridium pasteurianum] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=HCA:'>HCA</scene>, <scene name='pdbligand=CFM:'>CFM</scene> and <scene name='pdbligand=CLP:'>CLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MIO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Kim, J.]] | [[Category: Kim, J.]] | ||
| - | [[Category: Rees, D | + | [[Category: Rees, D C.]] |
[[Category: Woo, D.]] | [[Category: Woo, D.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: molybdenum-iron protein]] | [[Category: molybdenum-iron protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:30 2008'' |
Revision as of 11:55, 21 February 2008
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X-RAY CRYSTAL STRUCTURE OF THE NITROGENASE MOLYBDENUM-IRON PROTEIN FROM CLOSTRIDIUM PASTEURIANUM AT 3.0 ANGSTROMS RESOLUTION
Overview
The crystal structure of the nitrogenase molybdenum-iron (MoFe) protein from Clostridium pasteurianum (Cp1) has been determined at 3.0-A resolution by a combination of isomorphous replacement, molecular replacement, and noncrystallographic symmetry averaging. The structure of Cp1, including the two types of metal centers associated with the protein (the FeMo-cofactor and the P-cluster pair), is similar to that previously described for the MoFe-protein from Azotobacter vinelandii (Av1). Unique features of the Cp1 structure arise from the presence of an approximately 50-residue insertion in the alpha subunit and an approximately 50-residue deletion in the beta subunit. As a consequence, the FeMo-cofactor is more buried in Cp1 than in Av1, since the insertion is located on the surface above the FeMo-cofactor. The location of this insertion near the putative nitrogenase iron protein binding site provides a structural basis for the observation that the nitrogenase proteins from C. pasteurianum have low activity with complementary nitrogenase proteins isolated from other organisms. Mechanistic implications of the Cp1 structure for substrate entry/product release, substrate binding to the FeMo-cofactor, and electron- and proton-transfer reactions of nitrogenase are discussed.
About this Structure
1MIO is a Protein complex structure of sequences from Clostridium pasteurianum with , , and as ligands. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of the nitrogenase molybdenum-iron protein from Clostridium pasteurianum at 3.0-A resolution., Kim J, Woo D, Rees DC, Biochemistry. 1993 Jul 20;32(28):7104-15. PMID:8393705
Page seeded by OCA on Thu Feb 21 13:55:30 2008
Categories: Clostridium pasteurianum | Protein complex | Kim, J. | Rees, D C. | Woo, D. | CA | CFM | CLP | HCA | Molybdenum-iron protein
