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New page: left|200px<br /><applet load="1e8e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e8e" /> '''SOLUTION STRUCTURE OF METHYLOPHILUS METHYLOT... |
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== | ==Solution Structure of Methylophilus methylotrophus Cytochrome c''. Insights into the Structural Basis of Haem-Ligand Detachment== | ||
Cytochrome c" from Methylophilus methylotrophus is a monohaem protein with | <StructureSection load='1e8e' size='340' side='right'caption='[[1e8e]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1e8e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylophilus_methylotrophus Methylophilus methylotrophus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E8E FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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></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=1e8e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8e OCA], [https://pdbe.org/1e8e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e8e RCSB], [https://www.ebi.ac.uk/pdbsum/1e8e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8e ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CYCA_METME CYCA_METME] | |||
== 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/e8/1e8e_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1e8e ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cytochrome c" from Methylophilus methylotrophus is a monohaem protein with 124 amino acid residues. The iron has two histidine ligands in the oxidised form, one of which detaches and picks up a proton when the protein is reduced. Thus, both forms are paramagnetic. The structure of the oxidised form in solution, determined from NMR data is presented. The family of structures has an average backbone rmsd value of 0.53 A, and a heavy atom rmsd value of 0.95 A, within a target function range of 32 %. This structure is related to class I cytochromes with an additional helix at the N terminus. The haem-binding site occurs in a domain essentially lacking secondary structure motifs and the axial histidinyl residues were found in an unusual near perpendicular orientation. Moreover, a disulfide bridge is present, an uncommon structural feature among c-type cytochromes. The disulfide bridge, linking cysteine residues 96 and 104, forms a loop that confers rigidity and is essential to the detachment of the axial histidine (His95) as demonstrated by chemical disruption of the S-S bond. A route for protonation of the distal histidine involving haem propionate 17 is proposed and discussed in the light of available models for complex membrane proton pumps. | |||
Solution structure of Methylophilus methylotrophus cytochrome c": insights into the structural basis of haem-ligand detachment.,Brennan L, Turner DL, Fareleira P, Santos H J Mol Biol. 2001 Apr 27;308(2):353-65. PMID:11327772<ref>PMID:11327772</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1e8e" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methylophilus methylotrophus]] | [[Category: Methylophilus methylotrophus]] | ||
[[Category: Brennan L]] | |||
[[Category: Brennan | [[Category: Fareleira P]] | ||
[[Category: Fareleira | [[Category: Santos H]] | ||
[[Category: Santos | [[Category: Turner DL]] | ||
[[Category: Turner | |||
Latest revision as of 10:21, 23 October 2024
Solution Structure of Methylophilus methylotrophus Cytochrome c. Insights into the Structural Basis of Haem-Ligand DetachmentSolution Structure of Methylophilus methylotrophus Cytochrome c. Insights into the Structural Basis of Haem-Ligand Detachment
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCytochrome c" from Methylophilus methylotrophus is a monohaem protein with 124 amino acid residues. The iron has two histidine ligands in the oxidised form, one of which detaches and picks up a proton when the protein is reduced. Thus, both forms are paramagnetic. The structure of the oxidised form in solution, determined from NMR data is presented. The family of structures has an average backbone rmsd value of 0.53 A, and a heavy atom rmsd value of 0.95 A, within a target function range of 32 %. This structure is related to class I cytochromes with an additional helix at the N terminus. The haem-binding site occurs in a domain essentially lacking secondary structure motifs and the axial histidinyl residues were found in an unusual near perpendicular orientation. Moreover, a disulfide bridge is present, an uncommon structural feature among c-type cytochromes. The disulfide bridge, linking cysteine residues 96 and 104, forms a loop that confers rigidity and is essential to the detachment of the axial histidine (His95) as demonstrated by chemical disruption of the S-S bond. A route for protonation of the distal histidine involving haem propionate 17 is proposed and discussed in the light of available models for complex membrane proton pumps. Solution structure of Methylophilus methylotrophus cytochrome c": insights into the structural basis of haem-ligand detachment.,Brennan L, Turner DL, Fareleira P, Santos H J Mol Biol. 2001 Apr 27;308(2):353-65. PMID:11327772[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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