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| | <StructureSection load='3a5g' size='340' side='right'caption='[[3a5g]], [[Resolution|resolution]] 1.81Å' scene=''> | | <StructureSection load='3a5g' size='340' side='right'caption='[[3a5g]], [[Resolution|resolution]] 1.81Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3a5g]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tokunagayusurika_akamusi Tokunagayusurika akamusi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5G OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3A5G FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3a5g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tokunagayusurika_akamusi Tokunagayusurika akamusi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A5G FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 1.81Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2zwj|2zwj]], [[3a5a|3a5a]], [[3a5b|3a5b]], [[3a5h|3a5h]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</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'>[http://proteopedia.org/fgij/fg.htm?mol=3a5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5g OCA], [http://pdbe.org/3a5g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a5g RCSB], [http://www.ebi.ac.uk/pdbsum/3a5g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5g ProSAT]</span></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=3a5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5g OCA], [https://pdbe.org/3a5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a5g RCSB], [https://www.ebi.ac.uk/pdbsum/3a5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a5g ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q7M422_9DIPT Q7M422_9DIPT] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Tokunagayusurika akamusi]] | | [[Category: Tokunagayusurika akamusi]] |
| - | [[Category: Hasegawa, T]] | + | [[Category: Hasegawa T]] |
| - | [[Category: Kuwada, T]] | + | [[Category: Kuwada T]] |
| - | [[Category: Shishikura, F]] | + | [[Category: Shishikura F]] |
| - | [[Category: Takagi, T]] | + | [[Category: Takagi T]] |
| - | [[Category: Diptera]]
| + | |
| - | [[Category: Heme]]
| + | |
| - | [[Category: Hemoglobin]]
| + | |
| - | [[Category: Insect]]
| + | |
| - | [[Category: Midge larva]]
| + | |
| - | [[Category: Oxygen transport]]
| + | |
| - | [[Category: Propsilocerus akamusi]]
| + | |
| - | [[Category: Transport]]
| + | |
| Structural highlights
Function
Q7M422_9DIPT
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Haemoglobin component V (Hb V) from the midge larva Propsilocerus akamusi exhibits oxygen affinity despite the replacement of HisE7 and a pH-dependence of its functional properties. In order to understand the contribution of the distal residue to the ligand-binding properties and the pH-dependent structural changes in this insect Hb, the crystal structure of Hb V was determined under five different pH conditions. Structural comparisons of these Hb structures indicated that at neutral pH ArgE10 contributes to the stabilization of the haem-bound ligand molecule as a functional substitute for the nonpolar E7 residue. However, ArgE10 does not contribute to stabilization at acidic and alkaline pH because of the swinging movement of the Arg side chain under these conditions. This pH-dependent behaviour of Arg results in significant differences in the hydrogen-bond network on the distal side of the haem in the Hb V structures at different pH values. Furthermore, the change in pH results in a partial movement of the F helix, considering that coupled movements of ArgE10 and the F helix determine the haem location at each pH. These results suggested that Hb V retains its functional properties by adapting to the structural changes caused by amino-acid replacements.
pH-dependent structural changes in haemoglobin component V from the midge larva Propsilocerus akamusi (Orthocladiinae, Diptera).,Kuwada T, Hasegawa T, Takagi T, Sato I, Shishikura F Acta Crystallogr D Biol Crystallogr. 2010 Mar;66(Pt 3):258-67. Epub 2010, Feb 12. PMID:20179337[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kuwada T, Hasegawa T, Takagi T, Sato I, Shishikura F. pH-dependent structural changes in haemoglobin component V from the midge larva Propsilocerus akamusi (Orthocladiinae, Diptera). Acta Crystallogr D Biol Crystallogr. 2010 Mar;66(Pt 3):258-67. Epub 2010, Feb 12. PMID:20179337 doi:10.1107/S0907444909055760
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