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==Crystal structure of Parasponia hemoglobin; Differential Heme Coordination is Linked to Quaternary Structure==
==Crystal structure of Parasponia hemoglobin; Differential Heme Coordination is Linked to Quaternary Structure==
<StructureSection load='3qqr' size='340' side='right' caption='[[3qqr]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
<StructureSection load='3qqr' size='340' side='right'caption='[[3qqr]], [[Resolution|resolution]] 2.16&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3qqr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Parasponia_andersonii Parasponia andersonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QQR FirstGlance]. <br>
<table><tr><td colspan='2'>[[3qqr]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Parasponia_andersonii Parasponia andersonii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QQR FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qqr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qqr RCSB], [http://www.ebi.ac.uk/pdbsum/3qqr PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=3qqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qqr OCA], [https://pdbe.org/3qqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qqr RCSB], [https://www.ebi.ac.uk/pdbsum/3qqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qqr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/HBPL_PARAD HBPL_PARAD]] Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.  
[https://www.uniprot.org/uniprot/HBPL_PARAD HBPL_PARAD] Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Hemoglobins from the plants Parasponia andersonii (ParaHb) and Trema tomentosa (TremaHb) are 93% identical in primary structure but differ in oxygen binding constants in accordance with their distinct physiological functions. Additionally, these proteins are dimeric, and ParaHb exhibits the unusual property of having different heme redox potentials for each subunit. To investigate how these hemoglobins could differ in function despite their shared sequence identity, and to determine the cause of subunit heterogeneity in ParaHb, we have measured their crystal structures in the ferric oxidation state. Furthermore, we have made a monomeric ParaHb mutant protein (I43N) and measured its ferrous/ferric heme redox potential to test the hypothesized link between quaternary structure and heme heterogeneity in wild type ParaHb. Our results demonstrate that TremaHb is a symmetric dimeric hemoglobin similar to other class 1 nonsymbiotic plant hemoglobins, but that ParaHb has structurally distinct heme coordination in each of its two subunits that is absent in the monomeric I43N mutant protein. A mechanism for achieving structural heterogeneity in ParaHb is proposed, in which the Ile101(F4) side chain contacts the proximal His105(F8) in one subunit but not the other. These results are discussed in the context of the evolution of plant oxygen transport hemoglobins, and other potential functions of plant hemoglobins.
 
Crystal Structures of Parasponia and Trema Hemoglobins; Differential Heme Coordination is Linked to Quaternary Structure.,Kakar S, Sturms R, Tiffany A, Nix JC, Dispirito AA, Hargrove MS Biochemistry. 2011 Apr 14. PMID:21491905<ref>PMID:21491905</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Parasponia andersonii]]
[[Category: Parasponia andersonii]]
[[Category: Dispirito, A]]
[[Category: Dispirito A]]
[[Category: Hargrove, M S]]
[[Category: Hargrove MS]]
[[Category: Kakar, S]]
[[Category: Kakar S]]
[[Category: Nix, J C]]
[[Category: Nix JC]]
[[Category: Savage, A]]
[[Category: Savage A]]
[[Category: Sturms, R]]
[[Category: Sturms R]]
[[Category: Globin fold]]
[[Category: Oxygen transport]]

Latest revision as of 14:55, 14 March 2024

Crystal structure of Parasponia hemoglobin; Differential Heme Coordination is Linked to Quaternary StructureCrystal structure of Parasponia hemoglobin; Differential Heme Coordination is Linked to Quaternary Structure

Structural highlights

3qqr is a 2 chain structure with sequence from Parasponia andersonii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.16Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HBPL_PARAD Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.

See Also

3qqr, resolution 2.16Å

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