1i4y: Difference between revisions
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'''THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII WILD TYPE METHEMERYTHRIN''' | {{Structure | ||
|PDB= 1i4y |SIZE=350|CAPTION= <scene name='initialview01'>1i4y</scene>, resolution 1.80Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF PHASCOLOPSIS GOULDII WILD TYPE METHEMERYTHRIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1I4Y is a [ | 1I4Y is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phascolopsis_gouldii Phascolopsis gouldii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I4Y OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11372200 11372200] | ||
[[Category: Phascolopsis gouldii]] | [[Category: Phascolopsis gouldii]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxygen binding]] | [[Category: oxygen binding]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:45:38 2008'' | ||
Revision as of 09:45, 20 March 2008
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| 1i4y, resolution 1.80Å | |||||||||||||
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| Ligands: | CL and FEO | ||||||||||||
| 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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