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1JPB

Sperm Whale met-Myoglobin (low temperature; high pressure)

Summary for 1JPB
Entry DOI10.2210/pdb1jpb/pdb
Related1JP6 1JP8 1JP9
Descriptormyoglobin, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
Functional Keywordsoxygen storage/transport, oxygen storage-transport complex
Biological sourcePhyseter catodon (sperm whale)
Total number of polymer chains1
Total formula weight18235.69
Authors
Urayama, P.,Gruner, S.M.,Phillips Jr., G.N. (deposition date: 2001-08-01, release date: 2002-01-16, Last modification date: 2023-08-16)
Primary citationUrayama, P.,Phillips Jr., G.N.,Gruner, S.M.
Probing substates in sperm whale myoglobin using high-pressure crystallography.
Structure, 10:51-60, 2002
Cited by
PubMed Abstract: Pressures 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.
PubMed: 11796110
DOI: 10.1016/S0969-2126(01)00699-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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