1ajh

From Proteopedia

PHOTOPRODUCT OF CARBONMONOXY MYOGLOBIN AT 40 K

PDB ID 1ajh

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Structural highlights

1ajh is a 1 chain structure with sequence from Physeter catodon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.69Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

Myoglobin's reversible binding of oxygen is a model for studies of protein control of ligand binding and discrimination. Protein relaxation and geminate ligand rebinding subsequent to ligand photodissociation have been studied extensively by a variety of techniques. The ps to ns time scales for these processes are still much shorter than the ms time resolution of X-ray diffraction experiments, but it may be possible to trap these intermediates at low temperatures. We report here an X-ray diffraction investigation of structural changes induced by photolysis of carbonmonoxy myoglobin crystals at 40 K. Our results provide a structural basis for the interpretation of ambient and low temperature spectroscopic observations and molecular dynamics simulations of the ligand photodissociation and binding processes in haem proteins.

Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K.,Teng TY, Srajer V, Moffat K Nat Struct Biol. 1994 Oct;1(10):701-5. PMID:7634074^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Teng TY, Srajer V, Moffat K. Photolysis-induced structural changes in single crystals of carbonmonoxy myoglobin at 40 K. Nat Struct Biol. 1994 Oct;1(10):701-5. PMID:7634074