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1d8u

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[[Image:1d8u.gif|left|200px]]<br /><applet load="1d8u" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1d8u, resolution 2.35&Aring;" />
 
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'''CRYSTAL STRUCTURE OF NON-SYMBIOTIC PLANT HEMOGLOBIN FROM RICE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF NON-SYMBIOTIC PLANT HEMOGLOBIN FROM RICE==
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BACKGROUND: Nonsymbiotic hemoglobins (nsHbs) form a new class of plant proteins that is distinct genetically and structurally from leghemoglobins. They are found ubiquitously in plants and are expressed in low concentrations in a variety of tissues including roots and leaves. Their function involves a biochemical response to growth under limited O(2) conditions. RESULTS: The first X-ray crystal structure of a member of this class of proteins, riceHb1, has been determined to 2.4 A resolution using a combination of phasing techniques. The active site of ferric riceHb1 differs significantly from those of traditional hemoglobins and myoglobins. The proximal and distal histidine sidechains coordinate directly to the heme iron, forming a hemichrome with spectral properties similar to those of cytochrome b(5). The crystal structure also shows that riceHb1 is a dimer with a novel interface formed by close contacts between the G helix and the region between the B and C helices of the partner subunit. CONCLUSIONS: The bis-histidyl heme coordination found in riceHb1 is unusual for a protein that binds O(2) reversibly. However, the distal His73 is rapidly displaced by ferrous ligands, and the overall O(2) affinity is ultra-high (K(D) approximately 1 nM). Our crystallographic model suggests that ligand binding occurs by an upward and outward movement of the E helix, concomitant dissociation of the distal histidine, possible repacking of the CD corner and folding of the D helix. Although the functional relevance of quaternary structure in nsHbs is unclear, the role of two conserved residues in stabilizing the dimer interface has been identified.
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<StructureSection load='1d8u' size='340' side='right'caption='[[1d8u]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1d8u]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D8U FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<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></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1d8u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8u OCA], [https://pdbe.org/1d8u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d8u RCSB], [https://www.ebi.ac.uk/pdbsum/1d8u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d8u ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HBL1_ORYSJ HBL1_ORYSJ] May not function as an oxygen storage or transport protein, but might act as an oxygen sensor or play a role in electron transfer, possibly to a bound oxygen molecule. Has an unusually high affinity for O(2) because of a very low dissociation constant.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/d8/1d8u_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1d8u ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1D8U is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryza_sativa Oryza sativa] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8U OCA].
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*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Crystal structure of a nonsymbiotic plant hemoglobin., Hargrove MS, Brucker EA, Stec B, Sarath G, Arredondo-Peter R, Klucas RV, Olson JS, Phillips GN Jr, Structure. 2000 Sep 15;8(9):1005-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10986467 10986467]
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[[Category: Large Structures]]
[[Category: Oryza sativa]]
[[Category: Oryza sativa]]
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[[Category: Single protein]]
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[[Category: Brucker EA]]
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[[Category: Brucker, E A.]]
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[[Category: Hargrove M]]
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[[Category: Hargrove, M.]]
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[[Category: Olson JS]]
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[[Category: Jr., G N.Phillips.]]
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[[Category: Phillips Jr GN]]
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[[Category: Olson, J S.]]
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[[Category: Stec B]]
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[[Category: Stec, B.]]
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[[Category: HEM]]
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[[Category: bis-histidyl]]
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[[Category: globin]]
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[[Category: heme protein]]
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[[Category: oxygen storage/transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:14:09 2008''
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Current revision

CRYSTAL STRUCTURE OF NON-SYMBIOTIC PLANT HEMOGLOBIN FROM RICE

PDB ID 1d8u

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