View source for 8ugz


==Crystal structure of Shewanella benthica Group 1 truncated hemoglobin C51S C71S variant==
<StructureSection load='8ugz' size='340' side='right'caption='[[8ugz]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ugz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_benthica_KT99 Shewanella benthica KT99]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UGZ 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]] 1.8&#8491;</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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=8ugz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ugz OCA], [https://pdbe.org/8ugz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ugz RCSB], [https://www.ebi.ac.uk/pdbsum/8ugz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ugz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A9DF82_9GAMM A9DF82_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In our continued investigations of microbial globins, we solved the structure of a truncated hemoglobin from Shewanella benthica, an obligate psychropiezophilic bacterium. The distal side of the heme active site is lined mostly with hydrophobic residues, with the exception of a tyrosine, Tyr34 (CD1) and a histidine, His24 (B13). We found that purified SbHbN, when crystallized in the ferric form with polyethylene glycol as precipitant, turned into a green color over weeks. The electron density obtained from the green crystals accommodated a trans heme d, a chlorin-type derivative featuring a gamma-spirolactone and a vicinal hydroxyl group on a pyrroline ring. In solution, exposure of the protein to one equivalent of hydrogen peroxide resulted in a similar green color change, but caused by the formation of multiple products. These were oxidation species released on protein denaturation, likely including heme d, and a species with heme covalently attached to the polypeptide. The Tyr34Phe replacement prevented the formation of both heme d and the covalent linkage. The ready modification of heme b by SbHbN expands the range of chemistries supported by the globin fold and offers a route to a novel heme cofactor.

Heme d formation in a Shewanella benthica hemoglobin.,Martinez Grundman JE, Schultz TD, Schlessman JL, Liu K, Johnson EA, Lecomte JTJ J Inorg Biochem. 2024 Jun 27;259:112654. doi: 10.1016/j.jinorgbio.2024.112654. PMID:38959524<ref>PMID:38959524</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ugz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Shewanella benthica KT99]]
[[Category: Lecomte JTJ]]
[[Category: Martinez JE]]
[[Category: Schlessman JL]]
[[Category: Schultz TD]]
[[Category: Siegler MA]]