2c0e: Difference between revisions

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New page: left|200px<br /><applet load="2c0e" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c0e, resolution 2.35Å" /> '''STRUCTURE OF PDI-REL...
 
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[[Image:2c0e.gif|left|200px]]<br /><applet load="2c0e" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2c0e.gif|left|200px]]<br /><applet load="2c0e" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2c0e, resolution 2.35&Aring;" />
caption="2c0e, resolution 2.35&Aring;" />
'''STRUCTURE OF PDI-RELATED CHAPERONE, WIND WITH HIS-TAG ON C-TERMINUS.'''<br />
'''STRUCTURE OF PDI-RELATED CHAPERONE, WIND WITH HIS-TAG ON C-TERMINUS.'''<br />


==Overview==
==Overview==
The structures of the PDI-related protein Wind (with a C-terminal His(6), tag) and the mutants Y53S, Y53F and Y55K have been determined and compared, with the wild-type structure with the His(6) tag at the N-terminus. All, five structures show the same mode of dimerization, showing that this was, not an artefact introduced by the nearby N-terminal His(6) tag and, suggesting that this dimer may also be the biologically active form., Although the mutants Y53S and Y55K completely abrogate transport of the, protein Pipe (which appears to be the primary function of Wind in the, cell), only subtle differences can be seen in the putative Pipe-binding, region. The Pipe binding in the active forms appears to involve, hydrophobic interactions between aromatic systems, whereas the inactive, mutants may be able to bind more strongly with the help of hydrogen bonds, which could disturb the delicate equilibrium required for effective Pipe, transport.
The structures of the PDI-related protein Wind (with a C-terminal His(6) tag) and the mutants Y53S, Y53F and Y55K have been determined and compared with the wild-type structure with the His(6) tag at the N-terminus. All five structures show the same mode of dimerization, showing that this was not an artefact introduced by the nearby N-terminal His(6) tag and suggesting that this dimer may also be the biologically active form. Although the mutants Y53S and Y55K completely abrogate transport of the protein Pipe (which appears to be the primary function of Wind in the cell), only subtle differences can be seen in the putative Pipe-binding region. The Pipe binding in the active forms appears to involve hydrophobic interactions between aromatic systems, whereas the inactive mutants may be able to bind more strongly with the help of hydrogen bonds, which could disturb the delicate equilibrium required for effective Pipe transport.


==About this Structure==
==About this Structure==
2C0E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C0E OCA].  
2C0E is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C0E OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Barnewitz, K.]]
[[Category: Barnewitz, K.]]
[[Category: Ferrari, D.M.]]
[[Category: Ferrari, D M.]]
[[Category: Guo, C.]]
[[Category: Guo, C.]]
[[Category: Ma, Q.]]
[[Category: Ma, Q.]]
[[Category: Sevvana, M.]]
[[Category: Sevvana, M.]]
[[Category: Sheldrick, G.M.]]
[[Category: Sheldrick, G M.]]
[[Category: Soling, H.D.]]
[[Category: Soling, H D.]]
[[Category: chaperone]]
[[Category: chaperone]]
[[Category: developmental protein]]
[[Category: developmental protein]]
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[[Category: windbeutel]]
[[Category: windbeutel]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:58:38 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:32 2008''

Revision as of 17:43, 21 February 2008

File:2c0e.gif


2c0e, resolution 2.35Å

Drag the structure with the mouse to rotate

STRUCTURE OF PDI-RELATED CHAPERONE, WIND WITH HIS-TAG ON C-TERMINUS.

OverviewOverview

The structures of the PDI-related protein Wind (with a C-terminal His(6) tag) and the mutants Y53S, Y53F and Y55K have been determined and compared with the wild-type structure with the His(6) tag at the N-terminus. All five structures show the same mode of dimerization, showing that this was not an artefact introduced by the nearby N-terminal His(6) tag and suggesting that this dimer may also be the biologically active form. Although the mutants Y53S and Y55K completely abrogate transport of the protein Pipe (which appears to be the primary function of Wind in the cell), only subtle differences can be seen in the putative Pipe-binding region. The Pipe binding in the active forms appears to involve hydrophobic interactions between aromatic systems, whereas the inactive mutants may be able to bind more strongly with the help of hydrogen bonds, which could disturb the delicate equilibrium required for effective Pipe transport.

About this StructureAbout this Structure

2C0E is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

Structural elucidation of the PDI-related chaperone Wind with the help of mutants., Sevvana M, Biadene M, Ma Q, Guo C, Soling HD, Sheldrick GM, Ferrari DM, Acta Crystallogr D Biol Crystallogr. 2006 Jun;62(Pt 6):589-94. Epub 2006, May 12. PMID:16699185

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