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| | <StructureSection load='3wfw' size='340' side='right'caption='[[3wfw]], [[Resolution|resolution]] 1.65Å' scene=''> | | <StructureSection load='3wfw' size='340' side='right'caption='[[3wfw]], [[Resolution|resolution]] 1.65Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wfw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Meti4 Meti4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WFW OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3WFW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wfw]] is a 1 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=3WFW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WFW FirstGlance]. <br> |
| - | </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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3wfx|3wfx]]</div></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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hmp, Minf_1089 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=481448 METI4])</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=3wfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfw OCA], [https://pdbe.org/3wfw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wfw RCSB], [https://www.ebi.ac.uk/pdbsum/3wfw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfw ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3wfw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wfw OCA], [http://pdbe.org/3wfw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wfw RCSB], [http://www.ebi.ac.uk/pdbsum/3wfw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wfw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/B3DUZ1_METI4 B3DUZ1_METI4] |
| - | 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.
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| - | 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>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 3wfw" style="background-color:#fffaf0;"></div>
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| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Meti4]] | + | [[Category: Methylacidiphilum infernorum V4]] |
| - | [[Category: Teh, A H]] | + | [[Category: Teh AH]] |
| - | [[Category: Closed form]]
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| - | [[Category: Globin]]
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| - | [[Category: Oxygen transport]]
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| - | [[Category: Signalling]]
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