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==Lumbricus Erythrocruorin at 3.5A resolution== | |||
<StructureSection load='2gtl' size='340' side='right'caption='[[2gtl]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
| | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2gtl]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Lumbricus_terrestris Lumbricus terrestris]. The March 2013 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Erythrocruorin'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2013_3 10.2210/rcsb_pdb/mom_2013_3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GTL 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]] 3.5Å</td></tr> | |||
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2gtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gtl OCA], [https://pdbe.org/2gtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gtl RCSB], [https://www.ebi.ac.uk/pdbsum/2gtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gtl ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GLB4_LUMTE GLB4_LUMTE] | |||
== 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/gt/2gtl_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=2gtl ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Annelid erythrocruorins are highly cooperative extracellular respiratory proteins with molecular masses on the order of 3.6 million Daltons. We report here the 3.5 A crystal structure of erythrocruorin from the earthworm Lumbricus terrestris. This structure reveals details of symmetrical and quasi-symmetrical interactions that dictate the self-limited assembly of 144 hemoglobin and 36 linker subunits. The linker subunits assemble into a core complex with D(6) symmetry onto which 12 hemoglobin dodecamers bind to form the entire complex. Although the three unique linker subunits share structural similarity, their interactions with each other and the hemoglobin subunits display striking diversity. The observed diversity includes design features that have been incorporated into the linker subunits and may be critical for efficient assembly of large quantities of this complex respiratory protein. | Annelid erythrocruorins are highly cooperative extracellular respiratory proteins with molecular masses on the order of 3.6 million Daltons. We report here the 3.5 A crystal structure of erythrocruorin from the earthworm Lumbricus terrestris. This structure reveals details of symmetrical and quasi-symmetrical interactions that dictate the self-limited assembly of 144 hemoglobin and 36 linker subunits. The linker subunits assemble into a core complex with D(6) symmetry onto which 12 hemoglobin dodecamers bind to form the entire complex. Although the three unique linker subunits share structural similarity, their interactions with each other and the hemoglobin subunits display striking diversity. The observed diversity includes design features that have been incorporated into the linker subunits and may be critical for efficient assembly of large quantities of this complex respiratory protein. | ||
Lumbricus erythrocruorin at 3.5 A resolution: architecture of a megadalton respiratory complex.,Royer WE Jr, Sharma H, Strand K, Knapp JE, Bhyravbhatla B Structure. 2006 Jul;14(7):1167-77. PMID:16843898<ref>PMID:16843898</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 2gtl" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Erythrocruorin]] | |||
[[Category: Large Structures]] | |||
[[Category: Lumbricus terrestris]] | [[Category: Lumbricus terrestris]] | ||
[[Category: | [[Category: RCSB PDB Molecule of the Month]] | ||
[[Category: Bhyravbhatla | [[Category: Bhyravbhatla B]] | ||
[[Category: | [[Category: Knapp JE]] | ||
[[Category: | [[Category: Royer Jr WE]] | ||
[[Category: Sharma | [[Category: Sharma H]] | ||
[[Category: Strand | [[Category: Strand K]] | ||
Latest revision as of 11:05, 30 October 2024
Lumbricus Erythrocruorin at 3.5A resolutionLumbricus Erythrocruorin at 3.5A resolution
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAnnelid erythrocruorins are highly cooperative extracellular respiratory proteins with molecular masses on the order of 3.6 million Daltons. We report here the 3.5 A crystal structure of erythrocruorin from the earthworm Lumbricus terrestris. This structure reveals details of symmetrical and quasi-symmetrical interactions that dictate the self-limited assembly of 144 hemoglobin and 36 linker subunits. The linker subunits assemble into a core complex with D(6) symmetry onto which 12 hemoglobin dodecamers bind to form the entire complex. Although the three unique linker subunits share structural similarity, their interactions with each other and the hemoglobin subunits display striking diversity. The observed diversity includes design features that have been incorporated into the linker subunits and may be critical for efficient assembly of large quantities of this complex respiratory protein. Lumbricus erythrocruorin at 3.5 A resolution: architecture of a megadalton respiratory complex.,Royer WE Jr, Sharma H, Strand K, Knapp JE, Bhyravbhatla B Structure. 2006 Jul;14(7):1167-77. PMID:16843898[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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