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==Trematode hemoglobin from Paramphistomum epiclitum== | |||
<StructureSection load='1h97' size='340' side='right'caption='[[1h97]], [[Resolution|resolution]] 1.17Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1h97]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paramphistomum_epiclitum Paramphistomum epiclitum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H97 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H97 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]] 1.17Å</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=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=1h97 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h97 OCA], [https://pdbe.org/1h97 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h97 RCSB], [https://www.ebi.ac.uk/pdbsum/1h97 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h97 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GLB_PAREP GLB_PAREP] Oxygen binding protein. | |||
== 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/h9/1h97_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1h97 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Monomeric hemoglobin from the trematode Paramphistomum epiclitum displays very high oxygen affinity (P(50)<0.001 mm Hg) and an unusual heme distal site containing tyrosyl residues at the B10 and E7 positions. The crystal structure of aquo-met P. epiclitum hemoglobin, solved at 1.17 A resolution via multiwavelength anomalous dispersion techniques (R-factor=0.121), shows that the heme distal site pocket residue TyrB10 is engaged in hydrogen bonding to the iron-bound ligand. By contrast, residue TyrE7 is unexpectedly locked next to the CD globin region, in a conformation unsuitable for heme-bound ligand stabilisation. Such structural organization of the E7 distal residue differs strikingly from that observed in the nematode Ascaris suum hemoglobin (bearing TyrB10 and GlnE7 residues), which also displays very high oxygen affinity. The oxygenation and carbonylation parameters of wild-type P. epiclitum Hb as well as of single- and double-site mutants, with residue substitutions at positions B10, E7 and E11, have been determined and are discussed here in the light of the protein atomic resolution crystal structure. | |||
Very high resolution structure of a trematode hemoglobin displaying a TyrB10-TyrE7 heme distal residue pair and high oxygen affinity.,Pesce A, Dewilde S, Kiger L, Milani M, Ascenzi P, Marden MC, Van Hauwaert ML, Vanfleteren J, Moens L, Bolognesi M J Mol Biol. 2001 Jun 22;309(5):1153-64. PMID:11399085<ref>PMID:11399085</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1h97" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Paramphistomum epiclitum]] | [[Category: Paramphistomum epiclitum]] | ||
[[Category: Ascenzi P]] | |||
[[Category: Ascenzi | [[Category: Bolognesi M]] | ||
[[Category: Bolognesi | [[Category: Dewilde S]] | ||
[[Category: Dewilde | [[Category: Kiger L]] | ||
[[Category: Marden MC]] | |||
[[Category: Kiger | [[Category: Milani M]] | ||
[[Category: Marden | [[Category: Moens L]] | ||
[[Category: Milani | [[Category: Pesce A]] | ||
[[Category: Moens | [[Category: Van Hauwaert ML]] | ||
[[Category: Pesce | [[Category: Vanfleteren J]] | ||
[[Category: | |||
[[Category: | |||
Latest revision as of 11:54, 9 May 2024
Trematode hemoglobin from Paramphistomum epiclitumTrematode hemoglobin from Paramphistomum epiclitum
Structural highlights
FunctionGLB_PAREP Oxygen binding protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMonomeric hemoglobin from the trematode Paramphistomum epiclitum displays very high oxygen affinity (P(50)<0.001 mm Hg) and an unusual heme distal site containing tyrosyl residues at the B10 and E7 positions. The crystal structure of aquo-met P. epiclitum hemoglobin, solved at 1.17 A resolution via multiwavelength anomalous dispersion techniques (R-factor=0.121), shows that the heme distal site pocket residue TyrB10 is engaged in hydrogen bonding to the iron-bound ligand. By contrast, residue TyrE7 is unexpectedly locked next to the CD globin region, in a conformation unsuitable for heme-bound ligand stabilisation. Such structural organization of the E7 distal residue differs strikingly from that observed in the nematode Ascaris suum hemoglobin (bearing TyrB10 and GlnE7 residues), which also displays very high oxygen affinity. The oxygenation and carbonylation parameters of wild-type P. epiclitum Hb as well as of single- and double-site mutants, with residue substitutions at positions B10, E7 and E11, have been determined and are discussed here in the light of the protein atomic resolution crystal structure. Very high resolution structure of a trematode hemoglobin displaying a TyrB10-TyrE7 heme distal residue pair and high oxygen affinity.,Pesce A, Dewilde S, Kiger L, Milani M, Ascenzi P, Marden MC, Van Hauwaert ML, Vanfleteren J, Moens L, Bolognesi M J Mol Biol. 2001 Jun 22;309(5):1153-64. PMID:11399085[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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