1fp6
From Proteopedia
(New page: 200px<br /><applet load="1fp6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fp6, resolution 2.15Å" /> '''THE NITROGENASE FE P...) |
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| - | [[Image:1fp6.jpg|left|200px]]<br /><applet load="1fp6" size=" | + | [[Image:1fp6.jpg|left|200px]]<br /><applet load="1fp6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fp6, resolution 2.15Å" /> | caption="1fp6, resolution 2.15Å" /> | ||
'''THE NITROGENASE FE PROTEIN FROM AZOTOBACTER VINELANDII COMPLEXED WITH MGADP'''<br /> | '''THE NITROGENASE FE PROTEIN FROM AZOTOBACTER VINELANDII COMPLEXED WITH MGADP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Coupling the energy of nucleoside triphosphate binding and hydrolysis to | + | Coupling the energy of nucleoside triphosphate binding and hydrolysis to conformational changes is a common mechanism for a number of proteins with disparate cellular functions, including those involved in DNA replication, protein synthesis, and cell differentiation. Unique to this class of proteins is the dimeric Fe protein component of nitrogenase in which the binding and hydrolysis of MgATP controls intermolecular electron transfer and reduction of nitrogen to ammonia. In the work presented here, the MgADP-bound (or "off") conformational state of the nitrogenase Fe protein has been captured and a 2.15 A resolution X-ray crystal structure is presented. The structure described herein reveals likely mechanisms for long-range communication from the nucleotide-binding sites for controlling the affinity of association with the MoFe protein component. Two pathways, termed switches I and II, appear to be integral to this nucleotide signal transduction mechanism. In addition, the structure provides the basis for the changes in the biophysical properties of the [4Fe-4S] cluster observed when Fe protein binds nucleotides. The structure of the MgADP-bound Fe protein provides important insights into the respective contributions of nucleotide interaction and complex formation in defining the conformational states that are the keys to nitrogenase catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 1FP6 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 MG, SF4 and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] Full crystallographic information is available from [http:// | + | 1FP6 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=MG:'>MG</scene>, <scene name='pdbligand=SF4:'>SF4</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Nitrogenase Nitrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.18.6.1 1.18.6.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FP6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Nitrogenase]] | [[Category: Nitrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Jang, S | + | [[Category: Jang, S B.]] |
| - | [[Category: Peters, J | + | [[Category: Peters, J W.]] |
| - | [[Category: Seefeldt, L | + | [[Category: Seefeldt, L C.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: nuclotide]] | [[Category: nuclotide]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:41:05 2008'' |
Revision as of 10:41, 21 February 2008
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THE NITROGENASE FE PROTEIN FROM AZOTOBACTER VINELANDII COMPLEXED WITH MGADP
Overview
Coupling the energy of nucleoside triphosphate binding and hydrolysis to conformational changes is a common mechanism for a number of proteins with disparate cellular functions, including those involved in DNA replication, protein synthesis, and cell differentiation. Unique to this class of proteins is the dimeric Fe protein component of nitrogenase in which the binding and hydrolysis of MgATP controls intermolecular electron transfer and reduction of nitrogen to ammonia. In the work presented here, the MgADP-bound (or "off") conformational state of the nitrogenase Fe protein has been captured and a 2.15 A resolution X-ray crystal structure is presented. The structure described herein reveals likely mechanisms for long-range communication from the nucleotide-binding sites for controlling the affinity of association with the MoFe protein component. Two pathways, termed switches I and II, appear to be integral to this nucleotide signal transduction mechanism. In addition, the structure provides the basis for the changes in the biophysical properties of the [4Fe-4S] cluster observed when Fe protein binds nucleotides. The structure of the MgADP-bound Fe protein provides important insights into the respective contributions of nucleotide interaction and complex formation in defining the conformational states that are the keys to nitrogenase catalysis.
About this Structure
1FP6 is a Single protein structure of sequence from Azotobacter vinelandii with , and as ligands. Active as Nitrogenase, with EC number 1.18.6.1 Full crystallographic information is available from OCA.
Reference
Insights into nucleotide signal transduction in nitrogenase: structure of an iron protein with MgADP bound., Jang SB, Seefeldt LC, Peters JW, Biochemistry. 2000 Dec 5;39(48):14745-52. PMID:11101289
Page seeded by OCA on Thu Feb 21 12:41:05 2008
Categories: Azotobacter vinelandii | Nitrogenase | Single protein | Jang, S B. | Peters, J W. | Seefeldt, L C. | ADP | MG | SF4 | Av2 | Fe protein | Mgadp | Nitrogen fixation | Nuclotide
