1emy: Difference between revisions
New page: left|200px<br /><applet load="1emy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1emy, resolution 1.78Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1emy.gif|left|200px]]<br /><applet load="1emy" size=" | [[Image:1emy.gif|left|200px]]<br /><applet load="1emy" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1emy, resolution 1.78Å" /> | caption="1emy, resolution 1.78Å" /> | ||
'''CRYSTAL STRUCTURE OF ASIAN ELEPHANT (ELEPHAS MAXIMUS) CYANO-MET MYOGLOBIN AT 1.78 ANGSTROMS RESOLUTION. PHE 29 (B10) ACCOUNTS FOR ITS UNUSUAL LIGAND BINDING PROPERTIES'''<br /> | '''CRYSTAL STRUCTURE OF ASIAN ELEPHANT (ELEPHAS MAXIMUS) CYANO-MET MYOGLOBIN AT 1.78 ANGSTROMS RESOLUTION. PHE 29 (B10) ACCOUNTS FOR ITS UNUSUAL LIGAND BINDING PROPERTIES'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of Asian elephant cyano-metmyoglobin which has a | The crystal structure of Asian elephant cyano-metmyoglobin which has a glutamine instead of the usual distal site histidine has been determined to high resolution. In addition to this replacement, the substitution of a conserved leucine residue in position 29(B10) at the distal side by a phenylalanine was unambiguously identified based on the available electron density. The suspicion, that there were errors in the original sequence which has caused some confusion, is thus confirmed. Comparison with other myoglobin structures in various ligated forms reveals an essentially unchanged tertiary structure in elephant myoglobin despite the two amino acid substitutions in the heme pocket. Our current structural model shows that the N epsilon 2 atom of Gln64(E7) has moved with respect to the corresponding nitrogen position of His64(E7) in the CO complex of sperm whale myoglobin. The newly assigned residue Phe29(B10) penetrates into the distal side of the heme pocket approaching the ligand within van der Waals distance and causing a much more crowded heme pocket compared to other myoglobins. Kinetic properties of Asian elephant myoglobin, wild type, and recombinant sperm whale myoglobins are discussed in relation to the structural consequences of the two amino acid substitutions H64Q and L29F. | ||
==About this Structure== | ==About this Structure== | ||
1EMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elephas_maximus Elephas maximus] with CYN and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1EMY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elephas_maximus Elephas maximus] with <scene name='pdbligand=CYN:'>CYN</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EMY OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Elephas maximus]] | [[Category: Elephas maximus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bisig, D | [[Category: Bisig, D A.]] | ||
[[Category: Piontek, K.]] | [[Category: Piontek, K.]] | ||
[[Category: CYN]] | [[Category: CYN]] | ||
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[[Category: heme protein]] | [[Category: heme protein]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:29:25 2008'' | ||
Revision as of 13:29, 21 February 2008
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CRYSTAL STRUCTURE OF ASIAN ELEPHANT (ELEPHAS MAXIMUS) CYANO-MET MYOGLOBIN AT 1.78 ANGSTROMS RESOLUTION. PHE 29 (B10) ACCOUNTS FOR ITS UNUSUAL LIGAND BINDING PROPERTIES
OverviewOverview
The crystal structure of Asian elephant cyano-metmyoglobin which has a glutamine instead of the usual distal site histidine has been determined to high resolution. In addition to this replacement, the substitution of a conserved leucine residue in position 29(B10) at the distal side by a phenylalanine was unambiguously identified based on the available electron density. The suspicion, that there were errors in the original sequence which has caused some confusion, is thus confirmed. Comparison with other myoglobin structures in various ligated forms reveals an essentially unchanged tertiary structure in elephant myoglobin despite the two amino acid substitutions in the heme pocket. Our current structural model shows that the N epsilon 2 atom of Gln64(E7) has moved with respect to the corresponding nitrogen position of His64(E7) in the CO complex of sperm whale myoglobin. The newly assigned residue Phe29(B10) penetrates into the distal side of the heme pocket approaching the ligand within van der Waals distance and causing a much more crowded heme pocket compared to other myoglobins. Kinetic properties of Asian elephant myoglobin, wild type, and recombinant sperm whale myoglobins are discussed in relation to the structural consequences of the two amino acid substitutions H64Q and L29F.
About this StructureAbout this Structure
1EMY is a Single protein structure of sequence from Elephas maximus with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of Asian elephant (Elephas maximus) cyano-metmyoglobin at 1.78-A resolution. Phe29(B10) accounts for its unusual ligand binding properties., Bisig DA, Di Iorio EE, Diederichs K, Winterhalter KH, Piontek K, J Biol Chem. 1995 Sep 1;270(35):20754-62. PMID:7657658
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