1xcp

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[[Image:1xcp.gif|left|200px]]<br /><applet load="1xcp" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xcp.gif|left|200px]]
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caption="1xcp, resolution 3.2&Aring;" />
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'''Crystal Structure of the Nitrogenase Fe protein Phe135Trp with MgADP bound'''<br />
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{{Structure
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|PDB= 1xcp |SIZE=350|CAPTION= <scene name='initialview01'>1xcp</scene>, resolution 3.2&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''Crystal Structure of the Nitrogenase Fe protein Phe135Trp with MgADP bound'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1XCP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Azotobacter_vinelandii Azotobacter vinelandii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XCP OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15650336 15650336]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15650336 15650336]
[[Category: Azotobacter vinelandii]]
[[Category: Azotobacter vinelandii]]
[[Category: Nitrogenase]]
[[Category: Nitrogenase]]
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[[Category: mgadp]]
[[Category: mgadp]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:53:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:08:01 2008''

Revision as of 13:08, 20 March 2008

Image:1xcp.gif


PDB ID 1xcp

Drag the structure with the mouse to rotate
, resolution 3.2Å
Ligands: , and
Activity: Nitrogenase, with EC number 1.18.6.1
Coordinates: save as pdb, mmCIF, xml



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. 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

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