1i4y
From Proteopedia
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|PDB= 1i4y |SIZE=350|CAPTION= <scene name='initialview01'>1i4y</scene>, resolution 1.80Å | |PDB= 1i4y |SIZE=350|CAPTION= <scene name='initialview01'>1i4y</scene>, resolution 1.80Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1i4z|1I4Z]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4y OCA], [http://www.ebi.ac.uk/pdbsum/1i4y PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i4y RCSB]</span> | ||
}} | }} | ||
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[[Category: Rose, J.]] | [[Category: Rose, J.]] | ||
[[Category: Wang, B C.]] | [[Category: Wang, B C.]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: FEO]] | ||
[[Category: diiron]] | [[Category: diiron]] | ||
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| Line 34: | Line 35: | ||
[[Category: oxygen binding]] | [[Category: oxygen binding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:43 2008'' |
Revision as of 18:14, 30 March 2008
| |||||||
| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1I4Z
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII WILD TYPE METHEMERYTHRIN
Overview
Reported are the X-ray crystal structures of recombinant Phascolopsis gouldii methemerythrin (1.8-A resolution) and the structure of an O2-binding-pocket mutant, L98Y methemerythrin (2.1-A resolution). The L98Y hemerythrin (Hr) has a greatly enhanced O2 affinity, a slower O2 dissociation rate, a larger solvent deuterium isotope effect on this rate, and a greater resistance to autoxidation relative to the wild-type protein. The crystal structures show that the hydrophobic binding pocket of Hr can accommodate substitution of a leucyl by a tyrosyl side chain with relatively minor structural rearrangements. UV/vis and resonance Raman spectra show that in solution L98Y methemerythrin contains a mixture of two diiron site structures differing by the absence or presence of an Fe(III)-coordinated phenolate. However, in the crystal, only one L98Y diiron site structure is seen, in which the Y98 hydroxyl is not a ligand, but instead forms a hydrogen bond to a terminal hydroxo/aqua ligand to the nearest iron. Based on this crystal structure, we propose that in the oxy form of L98Y hemerythrin the non-polar nature of the binding pocket favors localization of the Y98 hydroxyl near the O2 binding site, where it can donate a hydrogen bond to the hydroperoxo ligand. The stabilizing Y98OH-O2H-interaction would account for all of the altered O2 binding properties of L98Y Hr listed above.
About this Structure
1I4Y is a Single protein structure of sequence from Phascolopsis gouldii. Full crystallographic information is available from OCA.
Reference
The crystal structures of Phascolopsis gouldii wild type and L98Y methemerythrins: structural and functional alterations of the O2 binding pocket., Farmer CS, Kurtz DM Jr, Liu ZJ, Wang BC, Rose J, Ai J, Sanders-Loehr J, J Biol Inorg Chem. 2001 Apr;6(4):418-29. PMID:11372200
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