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| | <StructureSection load='1n9f' size='340' side='right'caption='[[1n9f]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1n9f' size='340' side='right'caption='[[1n9f]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1n9f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1N9F FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1n9f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N9F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N9F 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=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1n9h|1n9h]], [[1n9i|1n9i]], [[1n9x|1n9x]], [[1naz|1naz]]</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=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Myoglobin ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 PHYCD])</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=1n9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9f OCA], [https://pdbe.org/1n9f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n9f RCSB], [https://www.ebi.ac.uk/pdbsum/1n9f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n9f 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=1n9f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n9f OCA], [http://pdbe.org/1n9f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n9f RCSB], [http://www.ebi.ac.uk/pdbsum/1n9f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n9f ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. | + | [https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phycd]] | + | [[Category: Physeter catodon]] |
| - | [[Category: Brunori, M]] | + | [[Category: Brunori M]] |
| - | [[Category: Federici, L]] | + | [[Category: Federici L]] |
| - | [[Category: Miele, A E]] | + | [[Category: Miele AE]] |
| - | [[Category: Sciara, G]] | + | [[Category: Sciara G]] |
| - | [[Category: Vallone, B]] | + | [[Category: Vallone B]] |
| - | [[Category: Globin fold]]
| + | |
| - | [[Category: Oxygen storage-transport complex]]
| + | |
| Structural highlights
Function
MYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
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
Crystals of the Met derivative of the sperm whale myoglobin triple mutant Mb-YQR [L(B10)Y, H(E7)Q and T(E10)R] were grown under microgravity conditions and on earth by vapour diffusion. A comparison of crystal quality after complete data collection and processing shows how microgravity-grown crystals diffract to better resolution and lead to considerably improved statistics for X-ray diffraction data compared with crystals grown on earth under the same conditions. The same set of experiments was reproduced on two different Spacelab missions (ISS 6A and ISS 8A) in 2001 and 2002. The structure of this mutant myoglobin, refined using data collected at ELETTRA (Trieste, Italy) from both kinds of crystals, shows that X-ray diffraction from microgravity-grown crystals leads to better defined electron-density maps as well as improved geometrical quality of the refined model. Improvement of the stereochemical parameters of a protein structure is fundamental to quantitative analysis of its function and dynamics and hence to thorough understanding of the molecular mechanisms of action.
Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutant.,Miele AE, Federici L, Sciara G, Draghi F, Brunori M, Vallone B Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):982-8. Epub 2003, May 23. PMID:12777759[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Miele AE, Federici L, Sciara G, Draghi F, Brunori M, Vallone B. Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutant. Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):982-8. Epub 2003, May 23. PMID:12777759
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