1ynr

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[[Image:1ynr.gif|left|200px]]
[[Image:1ynr.gif|left|200px]]
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{{Structure
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|PDB= 1ynr |SIZE=350|CAPTION= <scene name='initialview01'>1ynr</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1ynr", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|GENE=
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=COG4654 COG4654]</span>
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{{STRUCTURE_1ynr| PDB=1ynr | SCENE= }}
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|RELATEDENTRY=[[1ayg|1AYG]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ynr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ynr OCA], [http://www.ebi.ac.uk/pdbsum/1ynr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ynr RCSB]</span>
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'''Crystal structure of the cytochrome c-552 from Hydrogenobacter thermophilus at 2.0 resolution'''
'''Crystal structure of the cytochrome c-552 from Hydrogenobacter thermophilus at 2.0 resolution'''
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[[Category: Matteo, A Di.]]
[[Category: Matteo, A Di.]]
[[Category: Travaglini-Allocatelli, C.]]
[[Category: Travaglini-Allocatelli, C.]]
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[[Category: electron transport]]
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[[Category: Electron transport]]
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[[Category: helix]]
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[[Category: Helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:33:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:14:49 2008''
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Revision as of 13:33, 3 May 2008

Image:1ynr.gif

Template:STRUCTURE 1ynr

Crystal structure of the cytochrome c-552 from Hydrogenobacter thermophilus at 2.0 resolution


Overview

The folding mechanism of many proteins involves the population of partially organized structures en route to the native state. Identification and characterization of these intermediates is particularly difficult, as they are often only transiently populated and may play different mechanistic roles, being either on-pathway productive species or off-pathway kinetic traps. Following different spectroscopic probes, and employing state-of-the-art kinetic analysis, we present evidence that the folding mechanism of the thermostable cytochrome c552 from Hydrogenobacter thermophilus does involve the presence of an elusive, yet compact, on-pathway intermediate. Characterization of the folding mechanism of this cytochrome c is particularly interesting for the purpose of comparative folding studies, because H. thermophilus cytochrome c552 shares high sequence identity and structural homology with its homologue from the mesophilic bacterium Pseudomonas aeruginosa cytochrome c551, which refolds through a broad energy barrier without the accumulation of intermediates. Analysis of the folding kinetics and correlation with the three-dimensional structure add new evidence for the validity of a consensus folding mechanism in the cytochrome c family.

About this Structure

1YNR is a Single protein structure of sequence from Hydrogenobacter thermophilus. Full crystallographic information is available from OCA.

Reference

An obligatory intermediate in the folding pathway of cytochrome c552 from Hydrogenobacter thermophilus., Travaglini-Allocatelli C, Gianni S, Dubey VK, Borgia A, Di Matteo A, Bonivento D, Cutruzzola F, Bren KL, Brunori M, J Biol Chem. 2005 Jul 8;280(27):25729-34. Epub 2005 May 9. PMID:15883159 Page seeded by OCA on Sat May 3 16:33:20 2008

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