1lm0
From Proteopedia
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| - | [[Image:1lm0.gif|left|200px]] | + | [[Image:1lm0.gif|left|200px]] |
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| - | '''Solution structure and characterization of the heme chaperone CcmE''' | + | {{Structure |
| + | |PDB= 1lm0 |SIZE=350|CAPTION= <scene name='initialview01'>1lm0</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= ccmE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=24 Shewanella putrefaciens]) | ||
| + | }} | ||
| + | |||
| + | '''Solution structure and characterization of the heme chaperone CcmE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LM0 is a [ | + | 1LM0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_putrefaciens Shewanella putrefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LM0 OCA]. |
==Reference== | ==Reference== | ||
| - | Solution structure and characterization of the heme chaperone CcmE., Arnesano F, Banci L, Barker PD, Bertini I, Rosato A, Su XC, Viezzoli MS, Biochemistry. 2002 Nov 19;41(46):13587-94. PMID:[http:// | + | Solution structure and characterization of the heme chaperone CcmE., Arnesano F, Banci L, Barker PD, Bertini I, Rosato A, Su XC, Viezzoli MS, Biochemistry. 2002 Nov 19;41(46):13587-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12427019 12427019] |
[[Category: Shewanella putrefaciens]] | [[Category: Shewanella putrefaciens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ob-(oligonucleotide binding)fold]] | [[Category: ob-(oligonucleotide binding)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 12:32:25 2008'' |
Revision as of 10:32, 20 March 2008
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| Gene: | ccmE (Shewanella putrefaciens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure and characterization of the heme chaperone CcmE
Overview
The covalent attachment of the heme cofactor in c-type cytochromes is a surprisingly complex process, which in bacteria involves a number of different proteins. Among the latter, the ccmE gene product is known to perform a key role in the heme delivery pathway in Gram-negative bacteria. The solution structure of the soluble domain of apo-CcmE from Shewanella putrefaciens was determined through NMR spectroscopy on a 13C,15N-labeled sample. The structure is characterized by a compact core with large regions of beta structure, while the N-terminal and C-terminal regions are essentially unstructured. The overall folding is similar to that of the so-called oligo-binding proteins (OB fold). Solvent-exposed aromatic residues, conserved in all CcmE homologues, have been found in the proximity of His131, the putative heme-binding residue, that could have a role in the interaction with heme. No interaction between CcmE and heme, as well as between CcmE and holocytochrome c, could be detected in vitro by electronic spectroscopy or by NMR. The data available suggest that the heme transfer process is likely to involve a heterooligomeric protein complex and occur under a tight enzymatic control.
About this Structure
1LM0 is a Single protein structure of sequence from Shewanella putrefaciens. Full crystallographic information is available from OCA.
Reference
Solution structure and characterization of the heme chaperone CcmE., Arnesano F, Banci L, Barker PD, Bertini I, Rosato A, Su XC, Viezzoli MS, Biochemistry. 2002 Nov 19;41(46):13587-94. PMID:12427019
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