1fsl
From Proteopedia
(New page: 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=" | + | [[Image:1fsl.jpg|left|200px]]<br /><applet load="1fsl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1fsl, resolution 2.3Å" /> | caption="1fsl, resolution 2.3Å" /> | ||
'''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 | + | 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:// | + | 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 | + | [[Category: Ellis, P J.]] |
| - | [[Category: Freeman, H | + | [[Category: Freeman, H C.]] |
| - | [[Category: Guss, J | + | [[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:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:13 2008'' |
Revision as of 10:42, 21 February 2008
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FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE
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.
About this Structure
1FSL is a Single protein structure of sequence from Glycine max with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of ferric soybean leghemoglobin a nicotinate at 2.3 A resolution., Ellis PJ, Appleby CA, Guss JM, Hunter WN, Ollis DL, Freeman HC, Acta Crystallogr D Biol Crystallogr. 1997 May 1;53(Pt 3):302-10. PMID:15299933
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