1lm0

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[[Image:1lm0.gif|left|200px]]
[[Image:1lm0.gif|left|200px]]
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{{Structure
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|PDB= 1lm0 |SIZE=350|CAPTION= <scene name='initialview01'>1lm0</scene>
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|GENE= ccmE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=24 Shewanella putrefaciens])
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{{STRUCTURE_1lm0| PDB=1lm0 | SCENE= }}
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|RELATEDENTRY=[[1j6q|1J6Q]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lm0 OCA], [http://www.ebi.ac.uk/pdbsum/1lm0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lm0 RCSB]</span>
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'''Solution structure and characterization of the heme chaperone CcmE'''
'''Solution structure and characterization of the heme chaperone CcmE'''
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[[Category: Su, X C.]]
[[Category: Su, X C.]]
[[Category: Viezzoli, M S.]]
[[Category: Viezzoli, M S.]]
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[[Category: all-beta protein]]
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[[Category: All-beta protein]]
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[[Category: cytochrome c maturation]]
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[[Category: Cytochrome c maturation]]
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[[Category: heme delivery]]
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[[Category: Heme delivery]]
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[[Category: ob-(oligonucleotide binding)fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:03:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:27 2008''
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Revision as of 21:03, 2 May 2008

Template:STRUCTURE 1lm0

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 Page seeded by OCA on Sat May 3 00:03:05 2008

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