1ufp

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(New page: 200px<br /><applet load="1ufp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ufp, resolution 2.10&Aring;" /> '''Crystal Structure of...)
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caption="1ufp, resolution 2.10&Aring;" />
caption="1ufp, resolution 2.10&Aring;" />
'''Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-wild type Myoglobin'''<br />
'''Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-wild type Myoglobin'''<br />
==Overview==
==Overview==
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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.
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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==
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1UFP 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 PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UFP OCA].
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1UFP 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=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UFP OCA].
==Reference==
==Reference==
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[[Category: schiff base]]
[[Category: schiff base]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:05:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:00 2008''

Revision as of 13:24, 21 February 2008

Image:1ufp.jpg

1ufp, resolution 2.10Å

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Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-wild type Myoglobin

Overview

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

1UFP is a Single protein structure of sequence from Physeter catodon with as ligand. Full crystallographic information is available from OCA.

Reference

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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