2olp
From Proteopedia
(Difference between revisions)
(New page: 200px<br /><applet load="2olp" size="350" color="white" frame="true" align="right" spinBox="true" caption="2olp, resolution 1.932Å" /> '''Structure and ligan...) |
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| - | [[Image:2olp.jpg|left|200px]]<br /><applet load="2olp" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2olp, resolution 1.932Å" /> | ||
| - | '''Structure and ligand selection of hemoglobin II from Lucina pectinata'''<br /> | ||
| - | == | + | ==Structure and ligand selection of hemoglobin II from Lucina pectinata== |
| - | + | <StructureSection load='2olp' size='340' side='right'caption='[[2olp]], [[Resolution|resolution]] 1.93Å' scene=''> | |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2olp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Phacoides_pectinatus Phacoides pectinatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OLP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OLP 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]] 1.932Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2olp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2olp OCA], [https://pdbe.org/2olp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2olp RCSB], [https://www.ebi.ac.uk/pdbsum/2olp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2olp ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GLB2_PHAPT GLB2_PHAPT] | ||
| + | == 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/ol/2olp_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=2olp ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Lucina pectinata ctenidia harbor three heme proteins: sulfide-reactive hemoglobin I (HbI(Lp)) and the oxygen transporting hemoglobins II and III (HbII(Lp) and HbIII(Lp)) that remain unaffected by the presence of H(2)S. The mechanisms used by these three proteins for their function, including ligand control, remain unknown. The crystal structure of oxygen-bound HbII(Lp) shows a dimeric oxyHbII(Lp) where oxygen is tightly anchored to the heme through hydrogen bonds with Tyr(30)(B10) and Gln(65)(E7). The heme group is buried farther within HbII(Lp) than in HbI(Lp). The proximal His(97)(F8) is hydrogen bonded to a water molecule, which interacts electrostatically with a propionate group, resulting in a Fe-His vibration at 211 cm(-1). The combined effects of the HbII(Lp) small heme pocket, the hydrogen bonding network, the His(97) trans-effect, and the orientation of the oxygen molecule confer stability to the oxy-HbII(Lp) complex. Oxidation of HbI(Lp) Phe(B10) --> Tyr and HbII(Lp) only occurs when the pH is decreased from pH 7.5 to 5.0. Structural and resonance Raman spectroscopy studies suggest that HbII(Lp) oxygen binding and transport to the host bacteria may be regulated by the dynamic displacements of the Gln(65)(E7) and Tyr(30)(B10) pair toward the heme to protect it from changes in the heme oxidation state from Fe(II) to Fe(III). | ||
| - | + | Structure and ligand selection of hemoglobin II from Lucina pectinata.,Gavira JA, Camara-Artigas A, De Jesus-Bonilla W, Lopez-Garriga J, Lewis A, Pietri R, Yeh SR, Cadilla CL, Garcia-Ruiz JM J Biol Chem. 2008 Apr 4;283(14):9414-23. Epub 2008 Jan 18. PMID:18203714<ref>PMID:18203714</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2olp" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Phacoides pectinatus]] | ||
| + | [[Category: Camara-Artigas A]] | ||
| + | [[Category: Garcia-Ruiz JM]] | ||
| + | [[Category: Gavira JA]] | ||
| + | [[Category: Lopez-Garriga J]] | ||
| + | [[Category: De Jesus W]] | ||
Current revision
Structure and ligand selection of hemoglobin II from Lucina pectinata
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