1xcp
From Proteopedia
(New page: 200px<br /><applet load="1xcp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xcp, resolution 3.2Å" /> '''Crystal Structure of ...) |
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| - | [[Image:1xcp.gif|left|200px]]<br /><applet load="1xcp" size=" | + | [[Image:1xcp.gif|left|200px]]<br /><applet load="1xcp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xcp, resolution 3.2Å" /> | caption="1xcp, resolution 3.2Å" /> | ||
'''Crystal Structure of the Nitrogenase Fe protein Phe135Trp with MgADP bound'''<br /> | '''Crystal Structure of the Nitrogenase Fe protein Phe135Trp with MgADP bound'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the Azotobacter vinelandii nitrogenase Fe protein | + | The crystal structure of the Azotobacter vinelandii nitrogenase Fe protein with phenylalanine at position 135 substituted by tryptophan has been determined in MgADP-bound form by X-ray diffraction methods. Amino acid substitution studies have suggested that the phenylalanine at position 135 located near the [4Fe-4S] cluster contributes to both the midpoint potential and nucleotide-induced changes of the [4Fe-4S] cluster. Substitution of tryptophan for phenylalanine at position 135 resulted in a significant positive shift in the midpoint potential in both the isolated and nucleotide-bound states. The factors thought to control the midpoint potential of the [FeS] cluster include solvent accessibility, dipolar environment, and structural strain. The structure derived in the present work provides an explanation for the more positive midpoint potential observed in the nucleotide-bound state, and suggests important insights into the contributions of the nucleotide interaction to the conformational states that are the keys to nitrogenase catalysis. The presence of MgADP in Phe135Trp Fe protein reveals the mechanism of the long-range communication from the nucleotide-binding site that controls its affinity for the MoFe protein component. |
==About this Structure== | ==About this Structure== | ||
| - | 1XCP 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:// | + | 1XCP 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=1XCP 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: Jeong, M | + | [[Category: Jeong, M S.]] |
[[Category: ADP]] | [[Category: ADP]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: mgadp]] | [[Category: mgadp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:27 2008'' |
Revision as of 13:53, 21 February 2008
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Crystal Structure of the Nitrogenase Fe protein Phe135Trp with MgADP bound
Overview
The crystal structure of the Azotobacter vinelandii nitrogenase Fe protein with phenylalanine at position 135 substituted by tryptophan has been determined in MgADP-bound form by X-ray diffraction methods. Amino acid substitution studies have suggested that the phenylalanine at position 135 located near the [4Fe-4S] cluster contributes to both the midpoint potential and nucleotide-induced changes of the [4Fe-4S] cluster. Substitution of tryptophan for phenylalanine at position 135 resulted in a significant positive shift in the midpoint potential in both the isolated and nucleotide-bound states. The factors thought to control the midpoint potential of the [FeS] cluster include solvent accessibility, dipolar environment, and structural strain. The structure derived in the present work provides an explanation for the more positive midpoint potential observed in the nucleotide-bound state, and suggests important insights into the contributions of the nucleotide interaction to the conformational states that are the keys to nitrogenase catalysis. The presence of MgADP in Phe135Trp Fe protein reveals the mechanism of the long-range communication from the nucleotide-binding site that controls its affinity for the MoFe protein component.
About this Structure
1XCP 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
Structural basis for the changes in redox potential in the nitrogenase Phe135Trp Fe protein with MgADP Bound., Jeong MS, Jang SB, Mol Cells. 2004 Dec 31;18(3):374-82. PMID:15650336
Page seeded by OCA on Thu Feb 21 15:53:27 2008
Categories: Azotobacter vinelandii | Nitrogenase | Single protein | Jang, S B. | Jeong, M S. | ADP | MG | SF4 | F135w | Fe protein | Mgadp
