1sr3
From Proteopedia
(New page: 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=" | + | [[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 | + | 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 | + | 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]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:04:20 2008'' |
Revision as of 13:04, 21 February 2008
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Solution structure of the heme chaperone CcmE of Escherichia coli
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.
About this Structure
1SR3 is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1LIZ. Full crystallographic information is available from OCA.
Reference
NMR structure of the heme chaperone CcmE reveals a novel functional motif., Enggist E, Thony-Meyer L, Guntert P, Pervushin K, Structure. 2002 Nov;10(11):1551-7. PMID:12429096
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