View source for 3wfx


==Crystal Structure of the Imidazole-Bound Form of the HGbRL's Globin Domain==
<StructureSection load='3wfx' size='340' side='right'caption='[[3wfx]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wfx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylacidiphilum_infernorum_V4 Methylacidiphilum infernorum V4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WFX 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]] 1.94&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=HEZ:HEXANE-1,6-DIOL'>HEZ</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</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=3wfx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfx OCA], [https://pdbe.org/3wfx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wfx RCSB], [https://www.ebi.ac.uk/pdbsum/3wfx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/B3DUZ1_METI4 B3DUZ1_METI4] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Globins are haem-binding proteins with a conserved fold made up of alpha-helices and can possess diverse properties. A putative globin-coupled sensor from Methylacidiphilum infernorum, HGbRL, contains an N-terminal globin domain whose open and closed structures reveal an untypical dimeric architecture. Helices E and F fuse into an elongated helix, resulting in a novel site-swapped globin fold made up of helices A-E, hence the distal site, from one subunit and helices F-H, the proximal site, from another. The open structure possesses a large cavity binding an imidazole molecule, while the closed structure forms a unique Lys-His hexacoordinated species, with the first turn of helix E unravelling to allow Lys52(E10) to bind to the haem. Ligand binding induces reorganization of loop CE, which is stabilized in the closed form, and helix E, triggering a large conformational movement in the open form. These provide a mechanical insight into how a signal may be relayed between the globin domain and the C-terminal domain of HGbRL, a Roadblock/LC7 domain. Comparison with HGbI, a closely related globin, further underlines the high degree of structural versatility that the globin fold is capable of, enabling it to perform a diversity of functions.

Open and Lys-His Hexacoordinated Closed Structures of a Globin with Swapped Proximal and Distal Sites.,Teh AH, Saito JA, Najimudin N, Alam M Sci Rep. 2015 Jun 22;5:11407. doi: 10.1038/srep11407. PMID:26094577<ref>PMID:26094577</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wfx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Methylacidiphilum infernorum V4]]
[[Category: Teh AH]]