1fsl: Difference between revisions

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New page: left|200px<br /><applet load="1fsl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fsl, resolution 2.3Å" /> '''FERRIC SOYBEAN LEGHEM...
 
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[[Image:1fsl.jpg|left|200px]]<br /><applet load="1fsl" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fsl.jpg|left|200px]]<br /><applet load="1fsl" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fsl, resolution 2.3&Aring;" />
caption="1fsl, resolution 2.3&Aring;" />
'''FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE'''<br />
'''FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE'''<br />


==Overview==
==Overview==
Soybean leghemoglobin a is a small (16 kDa) protein facilitating the, transport of O(2) to respiring N(2)-fixing bacteria at low free-O(2), tension. The crystal structure of soybean ferric leghemoglobin a, nicotinate has been refined at 2.3 A resolution. The final R factor is, 15.8% for 6877 reflections between 6.0 and 2.3 A. The structure of soybean, leghemoglobin a (143 residues) is closely similar to that of lupin, leghemoglobin II (153 residues), the proteins having 82 identical residues, when the sequences are aligned. The new structure provides support for the, conclusion that the unique properties of leghemoglobin arise principally, from a heme pocket considerably larger and more flexible than that of, myoglobin, a strongly ruffled heme group, and a proximal histidine, orientation more favourable to ligand binding.
Soybean leghemoglobin a is a small (16 kDa) protein facilitating the transport of O(2) to respiring N(2)-fixing bacteria at low free-O(2) tension. The crystal structure of soybean ferric leghemoglobin a nicotinate has been refined at 2.3 A resolution. The final R factor is 15.8% for 6877 reflections between 6.0 and 2.3 A. The structure of soybean leghemoglobin a (143 residues) is closely similar to that of lupin leghemoglobin II (153 residues), the proteins having 82 identical residues when the sequences are aligned. The new structure provides support for the conclusion that the unique properties of leghemoglobin arise principally from a heme pocket considerably larger and more flexible than that of myoglobin, a strongly ruffled heme group, and a proximal histidine orientation more favourable to ligand binding.


==About this Structure==
==About this Structure==
1FSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] with HEM and NIO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FSL OCA].  
1FSL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=NIO:'>NIO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FSL OCA].  


==Reference==
==Reference==
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[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ellis, P.J.]]
[[Category: Ellis, P J.]]
[[Category: Freeman, H.C.]]
[[Category: Freeman, H C.]]
[[Category: Guss, J.M.]]
[[Category: Guss, J M.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: NIO]]
[[Category: NIO]]
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[[Category: respiratory protein]]
[[Category: respiratory protein]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:14:37 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:13 2008''