1ag6

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(New page: 200px<br /><applet load="1ag6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ag6, resolution 1.6&Aring;" /> '''PLASTOCYANIN FROM SPI...)
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[[Image:1ag6.jpg|left|200px]]<br /><applet load="1ag6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1ag6.jpg|left|200px]]<br /><applet load="1ag6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ag6, resolution 1.6&Aring;" />
caption="1ag6, resolution 1.6&Aring;" />
'''PLASTOCYANIN FROM SPINACH'''<br />
'''PLASTOCYANIN FROM SPINACH'''<br />
==Overview==
==Overview==
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The crystal structure of plastocyanin from spinach has been determined, using molecular replacement, with the structure of plastocyanin from, poplar as a search model. Successful crystallization was facilitated by, site-directed mutagenesis in which residue Gly8 was substituted with Asp., The region around residue 8 was believed to be too mobile for the, wild-type protein to form crystals despite extensive screening. The, current structure represents the oxidized plastocyanin, copper (II), at, low pH (approximately 4.4). In contrast to the similarity in the core, region as compared to its poplar counterpart, the structure shows some, significant differences in loop regions. The most notable is the large, shift of the 59-61 loop where the largest shift is 3.0 A for the C(alpha), atom of Glu59. This results in different patterns of electrostatic, potential around the acidic patches for the two proteins.
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The crystal structure of plastocyanin from spinach has been determined using molecular replacement, with the structure of plastocyanin from poplar as a search model. Successful crystallization was facilitated by site-directed mutagenesis in which residue Gly8 was substituted with Asp. The region around residue 8 was believed to be too mobile for the wild-type protein to form crystals despite extensive screening. The current structure represents the oxidized plastocyanin, copper (II), at low pH (approximately 4.4). In contrast to the similarity in the core region as compared to its poplar counterpart, the structure shows some significant differences in loop regions. The most notable is the large shift of the 59-61 loop where the largest shift is 3.0 A for the C(alpha) atom of Glu59. This results in different patterns of electrostatic potential around the acidic patches for the two proteins.
==About this Structure==
==About this Structure==
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1AG6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AG6 OCA].
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1AG6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea] with <scene name='pdbligand=CU:'>CU</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AG6 OCA].
==Reference==
==Reference==
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[[Category: electron transport]]
[[Category: electron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:49:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:44:10 2008''

Revision as of 09:44, 21 February 2008


1ag6, resolution 1.6Å

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PLASTOCYANIN FROM SPINACH

Overview

The crystal structure of plastocyanin from spinach has been determined using molecular replacement, with the structure of plastocyanin from poplar as a search model. Successful crystallization was facilitated by site-directed mutagenesis in which residue Gly8 was substituted with Asp. The region around residue 8 was believed to be too mobile for the wild-type protein to form crystals despite extensive screening. The current structure represents the oxidized plastocyanin, copper (II), at low pH (approximately 4.4). In contrast to the similarity in the core region as compared to its poplar counterpart, the structure shows some significant differences in loop regions. The most notable is the large shift of the 59-61 loop where the largest shift is 3.0 A for the C(alpha) atom of Glu59. This results in different patterns of electrostatic potential around the acidic patches for the two proteins.

About this Structure

1AG6 is a Single protein structure of sequence from Spinacia oleracea with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of spinach plastocyanin at 1.7 A resolution., Xue Y, Okvist M, Hansson O, Young S, Protein Sci. 1998 Oct;7(10):2099-105. PMID:9792096

Page seeded by OCA on Thu Feb 21 11:44:10 2008

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