1dly: Difference between revisions
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New page: left|200px<br /> <applet load="1dly" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dly, resolution 1.8Å" /> '''X-RAY CRYSTAL STRUCT... |
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== | ==X-RAY CRYSTAL STRUCTURE OF HEMOGLOBIN FROM THE GREEN UNICELLULAR ALGA CHLAMYDOMONAS EUGAMETOS== | ||
Small hemoproteins displaying amino acid sequences 20-40 residues shorter | <StructureSection load='1dly' size='340' side='right'caption='[[1dly]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1dly]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_moewusii Chlamydomonas moewusii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DLY 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]] 1.8Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <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=1dly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dly OCA], [https://pdbe.org/1dly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dly RCSB], [https://www.ebi.ac.uk/pdbsum/1dly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dly ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TRHN1_CHLMO TRHN1_CHLMO] | |||
== 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/dl/1dly_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=1dly ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Small hemoproteins displaying amino acid sequences 20-40 residues shorter than (non-)vertebrate hemoglobins (Hbs) have recently been identified in several pathogenic and non-pathogenic unicellular organisms, and named 'truncated hemoglobins' (trHbs). They have been proposed to be involved not only in oxygen transport but also in other biological functions, such as protection against reactive nitrogen species, photosynthesis or to act as terminal oxidases. Crystal structures of trHbs from the ciliated protozoan Paramecium caudatum and the green unicellular alga Chlamydomonas eugametos show that the tertiary structure of both proteins is based on a 'two-over-two' alpha-helical sandwich, reflecting an unprecedented editing of the classical 'three-over-three' alpha-helical globin fold. Based on specific Gly-Gly motifs the tertiary structure accommodates the deletion of the N-terminal A-helix and replacement of the crucial heme-binding F-helix with an extended polypeptide loop. Additionally, concerted structural modifications allow burying of the heme group and define the distal site, which hosts a TyrB10, GlnE7 residue pair. A set of structural and amino acid sequence consensus rules for stabilizing the fold and the bound heme in the trHbs homology subfamily is deduced. | |||
A novel two-over-two alpha-helical sandwich fold is characteristic of the truncated hemoglobin family.,Pesce A, Couture M, Dewilde S, Guertin M, Yamauchi K, Ascenzi P, Moens L, Bolognesi M EMBO J. 2000 Jun 1;19(11):2424-34. PMID:10835341<ref>PMID:10835341</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1dly" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Chlamydomonas moewusii]] | |||
[[Category: Large Structures]] | |||
[[Category: Bolognesi M]] | |||
[[Category: Couture M]] | |||
[[Category: Dewilde S]] | |||
[[Category: Guertin M]] | |||
[[Category: Moens L]] | |||
[[Category: Pesce A]] | |||
Latest revision as of 05:44, 13 August 2026
X-RAY CRYSTAL STRUCTURE OF HEMOGLOBIN FROM THE GREEN UNICELLULAR ALGA CHLAMYDOMONAS EUGAMETOS
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