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New page: left|200px<br /><applet load="1csv" size="450" color="white" frame="true" align="right" spinBox="true" caption="1csv, resolution 1.9Å" /> '''REPLACEMENTS IN A CON...
 
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'''REPLACEMENTS IN A CONSERVED LEUCINE CLUSTER IN THE HYDROPHOBIC HEME POCKET OF CYTOCHROME C'''<br />


==Overview==
==REPLACEMENTS IN A CONSERVED LEUCINE CLUSTER IN THE HYDROPHOBIC HEME POCKET OF CYTOCHROME C==
A cluster of highly conserved leucine side chains from residues 9, 68, 85, 94, and 98 is located in the hydrophobic heme pocket of cytochrome c. The, contributions of two of these, Leu 85 and Leu 94, have been studied using, a protein structure-function-mutagenesis approach to probe their roles in, the maintenance of overall structural integrity and electron transfer, activity. Structural studies of the L85C, L85F, L85M, and L94S mutant, proteins show that, in each case, the overall fold of cytochrome c is, retained, but that localized conformational shifts are required to, accommodate the introduced side chains. In particular, the side chains of, Cys 85 and Phe 85 form energetically favorable interactions with Phe 82, whereas Met 85 takes on a more remote conformation to prevent an, unfavorable interaction with the phenyl ring of Phe 82. In the case of the, L94S mutant protein, the new polar group introduced is found to form, hydrogen bonds to nearby carbonyl groups. In all proteins with, substitutions at Leu 85, the hydrophobic nature of the heme pocket is, preserved and no significant decrease in heme reduction potential is, observed. Despite earlier predictions that Leu 85 is an important, determinant in cytochrome c electron transfer partner complexation, our, studies show this is unlikely to be the case because the considerable, surface contour perturbations made by substitutions at this residue do not, correspondingly translate into significant changes in electron transfer, rates. For the L94S mutant protein, the substitution of a polar hydroxyl, group directly into the hydrophobic heme pocket has a larger effect on, heme reduction potential, but this is mitigated by two factors. First, the, side chain of Ser 94 is rotated away from the heme group and, second, the, side chain of Leu 98 shifts into a portion of the new space available, partially shielding the heme group. The Leu 94 Ser substitution does not, perturb the highly conserved interface formed by the nearly perpendicular, packing of the N- and C-terminal helices of cytochrome c, ruling this out, as the cause of this mutant protein becoming thermally labile and having a, lower functional activity. Our results show these effects are most likely, attributable to disruption of the heme pocket region. Much of the ability, of cytochrome c to absorb the introduction of mutations at Leu 85 and Leu, 94 appears to be a consequence of the conformational flexibility afforded, by the leucine cluster in this region as well as the presence of a nearby, internal cavity.(ABSTRACT TRUNCATED AT 400 WORDS)
<StructureSection load='1csv' size='340' side='right'caption='[[1csv]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1csv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CSV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CSV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1csv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1csv OCA], [https://pdbe.org/1csv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1csv RCSB], [https://www.ebi.ac.uk/pdbsum/1csv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1csv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CYC1_YEAST CYC1_YEAST] Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cs/1csv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1csv ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1CSV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4, HEM and TML as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CSV OCA].
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c., Lo TP, Murphy ME, Guillemette JG, Smith M, Brayer GD, Protein Sci. 1995 Feb;4(2):198-208. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7757009 7757009]
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Brayer GD]]
[[Category: Brayer, G.D.]]
[[Category: Lo TP]]
[[Category: Lo, T.P.]]
[[Category: HEM]]
[[Category: SO4]]
[[Category: TML]]
[[Category: electron transport(heme protein)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:44:06 2007''

Latest revision as of 18:42, 13 March 2024

REPLACEMENTS IN A CONSERVED LEUCINE CLUSTER IN THE HYDROPHOBIC HEME POCKET OF CYTOCHROME CREPLACEMENTS IN A CONSERVED LEUCINE CLUSTER IN THE HYDROPHOBIC HEME POCKET OF CYTOCHROME C

Structural highlights

1csv is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYC1_YEAST Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1csv, resolution 1.90Å

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