1jp9: Difference between revisions
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<StructureSection load='1jp9' size='340' side='right'caption='[[1jp9]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1jp9' size='340' side='right'caption='[[1jp9]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jp9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1jp9]] 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=1JP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JP9 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> | ||
<tr id=' | <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=SO4:SULFATE+ION'>SO4</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=1jp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jp9 OCA], [https://pdbe.org/1jp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jp9 RCSB], [https://www.ebi.ac.uk/pdbsum/1jp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jp9 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=1jp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jp9 OCA], [https://pdbe.org/1jp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jp9 RCSB], [https://www.ebi.ac.uk/pdbsum/1jp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jp9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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: | [[Category: Physeter catodon]] | ||
[[Category: Gruner | [[Category: Gruner SM]] | ||
[[Category: Phillips | [[Category: Phillips Jr GN]] | ||
[[Category: Urayama | [[Category: Urayama P]] | ||
Latest revision as of 11:43, 16 August 2023
Sperm Whale met-Myoglobin (low temperature; high pressure)Sperm Whale met-Myoglobin (low temperature; high pressure)
Structural highlights
FunctionMYG_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 PubMedPressures in the 100 MPa range are known to have an enormous number of effects on the action of proteins, but straightforward means for determining the structural basis of these effects have been lacking. Here, crystallography has been used to probe effects of pressure on sperm whale myoglobin structure. A comparison of pressure effects with those seen at low pH suggests that structural changes under pressure are interpretable as a shift in the populations of conformational substates. Furthermore, a novel high-pressure protein crystal-cooling method has been used to show low-temperature metastability, providing an alternative to room temperature, beryllium pressure cell-based techniques. The change in protein structure due to pressure is not purely compressive and involves conformational changes important to protein activity. Correlation with low-pH structures suggests observed structural changes are associated with global conformational substates. Methods developed here open up a direct avenue for exploration of the effects of pressure on proteins. Probing substates in sperm whale myoglobin using high-pressure crystallography.,Urayama P, Phillips GN Jr, Gruner SM Structure. 2002 Jan;10(1):51-60. PMID:11796110[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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