4g51: Difference between revisions
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==Crystallographic analysis of the interaction of nitric oxide with hemoglobin from Trematomus bernacchii in the T quaternary structure (fully ligated state).== | |||
<StructureSection load='4g51' size='340' side='right'caption='[[4g51]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4g51]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trematomus_bernacchii Trematomus bernacchii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G51 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]] 2.5Å</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=NO:NITRIC+OXIDE'>NO</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=4g51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g51 OCA], [https://pdbe.org/4g51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g51 RCSB], [https://www.ebi.ac.uk/pdbsum/4g51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g51 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HBA_TREBE HBA_TREBE] Involved in oxygen transport from gills to the various peripheral tissues. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Despite their high physiological relevance, haemoglobin crystal structures with NO bound to haem constitute less than 1% of the total ligated haemoglobins (Hbs) deposited in the Protein Data Bank. The major difficulty in obtaining NO-ligated Hbs is most likely to be related to the oxidative denitrosylation caused by the high reactivity of the nitrosylated species with O(2). Here, using Raman-assisted X-ray crystallography, it is shown that under X-ray exposure (at four different radiation doses) crystals of nitrosylated haemoglobin from Trematomus bernacchii undergo a transition, mainly in the beta chains, that generates a pentacoordinate species owing to photodissociation of the Fe-NO bond. These data provide a physical explanation for the low number of nitrosylated Hb structures available in the literature. | |||
Selective X-ray-induced NO photodissociation in haemoglobin crystals: evidence from a Raman-assisted crystallographic study.,Merlino A, Fuchs MR, Pica A, Balsamo A, Dworkowski FS, Pompidor G, Mazzarella L, Vergara A Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):137-40. doi:, 10.1107/S0907444912042229. Epub 2012 Dec 20. PMID:23275172<ref>PMID:23275172</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4g51" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Trematomus bernacchii]] | |||
[[Category: Balsamo A]] | |||
[[Category: Mazzarella L]] | |||
[[Category: Merlino A]] | |||
[[Category: Pica A]] | |||
[[Category: Vergara A]] | |||
Latest revision as of 10:52, 6 November 2024
Crystallographic analysis of the interaction of nitric oxide with hemoglobin from Trematomus bernacchii in the T quaternary structure (fully ligated state).
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