1fsl: Difference between revisions

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[[Image:1fsl.jpg|left|200px]]


{{Structure
==FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE==
|PDB= 1fsl |SIZE=350|CAPTION= <scene name='initialview01'>1fsl</scene>, resolution 2.3&Aring;
<StructureSection load='1fsl' size='340' side='right'caption='[[1fsl]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=NIO:NICOTINIC ACID'>NIO</scene>
<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>
|ACTIVITY=  
</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>
|GENE=  
<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.


'''FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE'''
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>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fsl" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
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.
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
 
== References ==
==About this Structure==
<references/>
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].
__TOC__
 
</StructureSection>
==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:[http://www.ncbi.nlm.nih.gov/pubmed/15299933 15299933]
[[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: HEM]]
[[Category: NIO]]
[[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 Thu Mar 20 11:13:29 2008''

Latest revision as of 06:00, 13 August 2026

FERRIC SOYBEAN LEGHEMOGLOBIN COMPLEXED WITH NICOTINATE

1fsl, resolution 2.30Å

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