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==CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROME== | ==CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROME== | ||
<StructureSection load='2mta' size='340' side='right' caption='[[2mta]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='2mta' size='340' side='right'caption='[[2mta]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2mta]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MTA OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[2mta]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17741 Atcc 17741]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MTA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2MTA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.1 1.4.9.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.1 1.4.9.1] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2mta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mta OCA], [http://pdbe.org/2mta PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mta RCSB], [http://www.ebi.ac.uk/pdbsum/2mta PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mta ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
*[[Cytochrome | *[[Cytochrome C 3D structures|Cytochrome C 3D structures]] | ||
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]] | *[[Methylamine dehydrogenase|Methylamine dehydrogenase]] | ||
== References == | == References == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 17741]] | [[Category: Atcc 17741]] | ||
[[Category: Large Structures]] | |||
[[Category: Chen, L]] | [[Category: Chen, L]] | ||
[[Category: Mathews, F S]] | [[Category: Mathews, F S]] | ||
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
Revision as of 09:28, 20 May 2020
CRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROMECRYSTAL STRUCTURE OF A TERNARY ELECTRON TRANSFER COMPLEX BETWEEN METHYLAMINE DEHYDROGENASE, AMICYANIN AND A C-TYPE CYTOCHROME
Structural highlights
Function[CYCL_PARDE] Electron acceptor for MDH. Acts in methanol oxidation. [DHMH_PARDE] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. [AMCY_PARDE] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin. [DHML_PARDE] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe crystal structure of a ternary protein complex has been determined at 2.4 angstrom resolution. The complex is composed of three electron transfer proteins from Paracoccus denitrificans, the quinoprotein methylamine dehydrogenase, the blue copper protein amicyanin, and the cytochrome c551i. The central region of the c551i is folded similarly to several small bacterial c-type cytochromes; there is a 45-residue extension at the amino terminus and a 25-residue extension at the carboxyl terminus. The methylamine dehydrogenase-amicyanin interface is largely hydrophobic, whereas the amicyanin-cytochrome interface is more polar, with several charged groups present on each surface. Analysis of the simplest electron transfer pathways between the redox partners points out the importance of other factors such as energetics in determining the electron transfer rates. Structure of an electron transfer complex: methylamine dehydrogenase, amicyanin, and cytochrome c551i.,Chen L, Durley RC, Mathews FS, Davidson VL Science. 1994 Apr 1;264(5155):86-90. PMID:8140419[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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