1sr3: Difference between revisions

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New page: left|200px<br /><applet load="1sr3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sr3" /> '''Solution structure of the heme chaperone Ccm...
 
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[[Image:1sr3.gif|left|200px]]<br /><applet load="1sr3" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1sr3.gif|left|200px]]<br /><applet load="1sr3" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1sr3" />
caption="1sr3" />
'''Solution structure of the heme chaperone CcmE of Escherichia coli'''<br />
'''Solution structure of the heme chaperone CcmE of Escherichia coli'''<br />


==Overview==
==Overview==
The concept of metal chaperones involves transient binding of metallic, cofactors by specific proteins for delivery to enzymes in which they, function. Metal chaperones thus provide a protective, as well as a, transport, function. We report the first structure of a heme chaperone, CcmE, which comprises these two functions. We propose that the covalent, attachment of heme to an exposed histidine occurs after heme binding at, the surface of a rigid molecule with a flexible C-terminal domain. CcmE, belongs to a family of proteins with a specific fold, which all share a, function in delivery of specific molecular cargo.
The concept of metal chaperones involves transient binding of metallic cofactors by specific proteins for delivery to enzymes in which they function. Metal chaperones thus provide a protective, as well as a transport, function. We report the first structure of a heme chaperone, CcmE, which comprises these two functions. We propose that the covalent attachment of heme to an exposed histidine occurs after heme binding at the surface of a rigid molecule with a flexible C-terminal domain. CcmE belongs to a family of proteins with a specific fold, which all share a function in delivery of specific molecular cargo.


==About this Structure==
==About this Structure==
1SR3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure superseeds the now removed PDB entry 1LIZ. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SR3 OCA].  
1SR3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1LIZ. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SR3 OCA].  


==Reference==
==Reference==
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[[Category: ob fold]]
[[Category: ob fold]]


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