1ufj: Difference between revisions
New page: left|200px<br /><applet load="1ufj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ufj, resolution 1.60Å" /> '''Crystal Structure of... |
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[[Image:1ufj.gif|left|200px]]<br /><applet load="1ufj" size=" | [[Image:1ufj.gif|left|200px]]<br /><applet load="1ufj" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ufj, resolution 1.60Å" /> | caption="1ufj, resolution 1.60Å" /> | ||
'''Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin'''<br /> | '''Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin'''<br /> | ||
==Overview== | ==Overview== | ||
Apo-myoglobin (apo-Mb) and apo-A71GMb were successfully reconstituted with | Apo-myoglobin (apo-Mb) and apo-A71GMb were successfully reconstituted with FeIII(salophen) (1) (salophen = N,N'-bis(salicylidene)-1,2-phenilenediamine), Fe(III)(3,3'-Me2-salophen) (2), and FeIII(5,5'-t-Bu2-salophen) (3). The crystal structure of 2.apo-A71GMb shows the tight binding of the complex in the Mb cavity, while in wild-type apo-Mb it is highly disordered due to the steric repulsion with Ala71. Furthermore, the structure of 2.apo-A71GMb suggests a possible accommodation of a small substrate in the cavity. In fact, the cyanide association rate constant of 2.apo-A71GMb is 216-fold larger compared to that of 2.apo-Mb. These results provide us principles for the noncovalent fixation of synthetic metal cofactors at the desired positions in protein matrixes. | ||
==About this Structure== | ==About this Structure== | ||
1UFJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with FE, PO4 and CZM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1UFJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=CZM:'>CZM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UFJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: schiff base]] | [[Category: schiff base]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:56 2008'' | ||
Revision as of 16:23, 21 February 2008
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Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin
OverviewOverview
Apo-myoglobin (apo-Mb) and apo-A71GMb were successfully reconstituted with FeIII(salophen) (1) (salophen = N,N'-bis(salicylidene)-1,2-phenilenediamine), Fe(III)(3,3'-Me2-salophen) (2), and FeIII(5,5'-t-Bu2-salophen) (3). The crystal structure of 2.apo-A71GMb shows the tight binding of the complex in the Mb cavity, while in wild-type apo-Mb it is highly disordered due to the steric repulsion with Ala71. Furthermore, the structure of 2.apo-A71GMb suggests a possible accommodation of a small substrate in the cavity. In fact, the cyanide association rate constant of 2.apo-A71GMb is 216-fold larger compared to that of 2.apo-Mb. These results provide us principles for the noncovalent fixation of synthetic metal cofactors at the desired positions in protein matrixes.
About this StructureAbout this Structure
1UFJ is a Single protein structure of sequence from Physeter catodon with , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structures of artificial metalloproteins: tight binding of FeIII(Schiff-Base) by mutation of Ala71 to Gly in apo-myoglobin., Ueno T, Ohashi M, Kono M, Kondo K, Suzuki A, Yamane T, Watanabe Y, Inorg Chem. 2004 May 3;43(9):2852-8. PMID:15106972
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