4xxl: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='4xxl' size='340' side='right'caption='[[4xxl]], [[Resolution|resolution]] 1.47Å' scene=''> | <StructureSection load='4xxl' size='340' side='right'caption='[[4xxl]], [[Resolution|resolution]] 1.47Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xxl]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xxl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sideroxydans_lithotrophicus_ES-1 Sideroxydans lithotrophicus ES-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XXL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XXL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEC:HEME+C'>HEC</scene> | </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=4xxl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xxl OCA], [https://pdbe.org/4xxl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xxl RCSB], [https://www.ebi.ac.uk/pdbsum/4xxl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xxl ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/D5CN26_SIDLE D5CN26_SIDLE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 25: | Line 26: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Sideroxydans lithotrophicus ES-1]] | ||
[[Category: Beckwith | [[Category: Beckwith CR]] | ||
[[Category: Clarke | [[Category: Clarke T]] | ||
[[Category: Edwards | [[Category: Edwards MJ]] | ||
Revision as of 20:57, 26 April 2023
Crystal structure of Class 1 cytochrome MtoD from Sideroxydans lithotrophicus ES-1Crystal structure of Class 1 cytochrome MtoD from Sideroxydans lithotrophicus ES-1
Structural highlights
FunctionPublication Abstract from PubMedThe autotrophic Sideroxydans lithotrophicus ES-1 can grow by coupling the oxidation of ferrous iron to the reduction of oxygen. Soluble ferrous iron is oxidized at the surface of the cell by an MtoAB porin-cytochrome complex that functions as an electron conduit through the outer membrane. Electrons are then transported to the cytoplasmic membrane where they are used to generate proton motive force (PMF) (for ATP synthesis) and NADH for autotrophic processes such as carbon fixation. As part of the mtoAB gene cluster, S. lithotrophicus also contains the gene mtoD that is proposed to encode a cytochrome c protein. We isolated mtoD from a Shewanella oneidensis expression system where the mtoD gene was expressed on a pBAD plasmid vector. Biochemical, biophysical, and crystallographic characterization of the purified MtoD revealed it as an 11 kDa monomeric protein containing a single heme. Sequence and structural alignment indicated that MtoD belonged to the class-1 cytochrome c family and had a similar fold to ferricytochrome c552 family, however the MtoD heme is bis-histidine coordinated and is substantially more exposed than the hemes of other family members. The reduction potential of the MtoD heme at pH 7 was +155 mV vs. Standard Hydrogen Electrode, which is approximately 100 mV lower than that of mitochondrial cytochrome c. Consideration of the properties of MtoD in the context of the potential respiratory partners identified from the genome suggests that MtoD could associate to multiple electron transfer partners as the primary periplasmic electron shuttle. Characterization of MtoD from Sideroxydans lithotrophicus: a cytochrome c electron shuttle used in lithoautotrophic growth.,Beckwith CR, Edwards MJ, Lawes M, Shi L, Butt JN, Richardson DJ, Clarke TA Front Microbiol. 2015 Apr 28;6:332. doi: 10.3389/fmicb.2015.00332. eCollection, 2015. PMID:25972843[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||