4v93
From Proteopedia
(Difference between revisions)
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<SX load='4v93' size='340' side='right' viewer='molstar' caption='[[4v93]], [[Resolution|resolution]] 8.10Å' scene=''> | <SX load='4v93' size='340' side='right' viewer='molstar' caption='[[4v93]], [[Resolution|resolution]] 8.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4v93]] is a 180 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[4v93]] is a 180 chain structure with sequence from [https://en.wikipedia.org/wiki/Lumbricus_terrestris Lumbricus terrestris]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4cyx 4cyx], [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d0h 4d0h] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4d0i 4d0i]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V93 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V93 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </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=4v93 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v93 OCA], [https://pdbe.org/4v93 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v93 RCSB], [https://www.ebi.ac.uk/pdbsum/4v93 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v93 ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GLB4_LUMTE GLB4_LUMTE] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The iron-containing hemoglobins (Hbs) are essential proteins to serve as oxygen transporters in the blood. Among various kinds of Hbs, the earthworm Hbs are the champions in carrying oxygen due to not only their large size but also the unusually high cooperativity of ligand binding. However, the cooperative oxygen binding mechanisms are still mostly unknown. Here we report the cryo-electron microscopy structure of Lumbricus terrestris Hb in its native, oxygenated state at 9.1 A resolution, showing remarkable differences from the carbon monoxide-binding X-ray structure. Our structural analysis first indicates that the cooperative ligand binding of L. terrestris Hb requires tertiary and quaternary transitions in the heme pocket and a global subunit movement facilitated by intra-ring and inter-ring contacts. Moreover, the additional sinusoidal bracelet provides the confirmation for the long-standing debate about the additional electron densities absent in the X-ray crystal structure. | ||
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| + | Structural basis for cooperative oxygen binding and bracelet-assisted assembly of Lumbricus terrestris hemoglobin.,Chen WT, Chen YC, Liou HH, Chao CY Sci Rep. 2015 Apr 21;5:9494. doi: 10.1038/srep09494. PMID:25897633<ref>PMID:25897633</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4v93" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</SX> | </SX> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Lumbricus terrestris]] | [[Category: Lumbricus terrestris]] | ||
| - | [[Category: Chao | + | [[Category: Chao CY]] |
| - | [[Category: Chen | + | [[Category: Chen WT]] |
| - | [[Category: Chen | + | [[Category: Chen YC]] |
| - | [[Category: Liou | + | [[Category: Liou HH]] |
| - | + | ||
Current revision
Fitted coordinates for Lumbricus terrestris hemoglobin cryo-EM complex (EMD-2627)
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