1sr3
From Proteopedia
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| - | [[Image:1sr3.gif|left|200px]] | + | [[Image:1sr3.gif|left|200px]] |
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| - | '''Solution structure of the heme chaperone CcmE of Escherichia coli''' | + | {{Structure |
| + | |PDB= 1sr3 |SIZE=350|CAPTION= <scene name='initialview01'>1sr3</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= CCME ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of the heme chaperone CcmE of Escherichia coli''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1SR3 is a [ | + | 1SR3 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12429096 12429096] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ob fold]] | [[Category: ob fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:08:35 2008'' |
Revision as of 12:08, 20 March 2008
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| Gene: | CCME (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 14:08:35 2008
