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[[Image:1fsl.jpg|left|200px]]
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{{STRUCTURE_1fsl|  PDB=1fsl  |  SCENE=  }}
'''FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE'''


==FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE==
<StructureSection load='1fsl' size='340' side='right'caption='[[1fsl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fsl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FSL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NIO:NICOTINIC+ACID'>NIO</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fsl OCA], [https://pdbe.org/1fsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fsl RCSB], [https://www.ebi.ac.uk/pdbsum/1fsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fsl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LGB3_SOYBN LGB3_SOYBN] Leghemoglobin that reversibly binds oxygen O(2) through a pentacoordinated heme iron (PubMed:29100196). In root nodules, facilitates the diffusion of oxygen to the bacteroids while preventing the bacterial nitrogenase from being inactivated by buffering dioxygen, nitric oxide and carbon monoxide, and promoting the formation of reactive oxygen species (ROS, e.g. H(2)O(2)) (PubMed:17540516, PubMed:22308405, PubMed:29701804, PubMed:32297921). This role is essential for symbiotic nitrogen fixation (SNF) (PubMed:17540516, PubMed:32297921).<ref>PMID:22308405</ref> <ref>PMID:29100196</ref> <ref>PMID:29701804</ref> <ref>PMID:32297921</ref> <ref>PMID:17540516</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fs/1fsl_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fsl ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:15299933</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1FSL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FSL OCA].
</div>
<div class="pdbe-citations 1fsl" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/15299933 15299933]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Ellis, P J.]]
[[Category: Ellis PJ]]
[[Category: Freeman, H C.]]
[[Category: Freeman HC]]
[[Category: Guss, J M.]]
[[Category: Guss JM]]
[[Category: Heme]]
[[Category: Multigene family]]
[[Category: Nitrogen fixation]]
[[Category: Oxygen transport]]
[[Category: Respiratory protein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 16:43:07 2008''

Latest revision as of 06:00, 13 August 2026

FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE

1fsl, resolution 2.30Å

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