1t9p

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[[Image:1t9p.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1t9p", creates the "Structure Box" on the page.
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{{STRUCTURE_1t9p| PDB=1t9p | SCENE= }}
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|RELATEDENTRY=[[1t9o|1T9O]], [[1t9q|1T9Q]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t9p OCA], [http://www.ebi.ac.uk/pdbsum/1t9p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t9p RCSB]</span>
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'''Crystal Structure of V44A, G45P Cp Rubredoxin'''
'''Crystal Structure of V44A, G45P Cp Rubredoxin'''
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[[Category: Smith, E T.]]
[[Category: Smith, E T.]]
[[Category: Youn, B.]]
[[Category: Youn, B.]]
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[[Category: rubredoxin]]
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[[Category: Rubredoxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:42:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:53:16 2008''
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Revision as of 06:42, 3 May 2008

Template:STRUCTURE 1t9p

Crystal Structure of V44A, G45P Cp Rubredoxin


Overview

Understanding the structural origins of differences in reduction potentials is crucial to understanding how various electron transfer proteins modulate their reduction potentials and how they evolve for diverse functional roles. Here, the high-resolution structures of several Clostridium pasteurianum rubredoxin (Cp Rd) variants with changes in the vicinity of the redox site are reported in order to increase this understanding. Our crystal structures of [V44L] (at 1.8 A resolution), [V44A] (1.6 A), [V44G] (2.0 A) and [V44A, G45P] (1.5 A) Rd (all in their oxidized states) show that there is a gradual decrease in the distance between Fe and the amide nitrogen of residue 44 upon reduction in the size of the side chain of residue 44; the decrease occurs from leucine to valine, alanine or glycine and is accompanied by a gradual increase in their reduction potentials. Mutation of Cp Rd at position 44 also changes the hydrogen-bond distance between the amide nitrogen of residue 44 and the sulfur of cysteine 42 in a size-dependent manner. Our results suggest that residue 44 is an important determinant of Rd reduction potential in a manner dictated by side-chain size. Along with the electric dipole moment of the 43-44 peptide bond and the 44-42 NH--S type hydrogen bond, a modulation mechanism for solvent accessibility through residue 41 might regulate the redox reaction of the Rds.

About this Structure

1T9P is a Single protein structure of sequence from Clostridium pasteurianum. Full crystallographic information is available from OCA.

Reference

Crystallographic studies of V44 mutants of Clostridium pasteurianum rubredoxin: effects of side-chain size on reduction potential., Park IY, Eidsness MK, Lin IJ, Gebel EB, Youn B, Harley JL, Machonkin TE, Frederick RO, Markley JL, Smith ET, Ichiye T, Kang C, Proteins. 2004 Nov 15;57(3):618-25. PMID:15382226 Page seeded by OCA on Sat May 3 09:42:51 2008

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