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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]] 2.40&Aring;' scene=''>
<StructureSection load='2mta' size='340' side='right'caption='[[2mta]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mta]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MTA FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mta]] is a 4 chain structure with sequence from [https://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 [https://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=HEC:HEME+C'>HEC</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/Amine_dehydrogenase Amine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.3 1.4.99.3] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [https://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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mta OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2mta RCSB], [http://www.ebi.ac.uk/pdbsum/2mta PDBsum]</span></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=2mta FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mta OCA], [https://pdbe.org/2mta PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mta RCSB], [https://www.ebi.ac.uk/pdbsum/2mta PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mta ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CYCL_PARDE CYCL_PARDE]] Electron acceptor for MDH. Acts in methanol oxidation. [[http://www.uniprot.org/uniprot/DHMH_PARDE DHMH_PARDE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. [[http://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE]] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin. [[http://www.uniprot.org/uniprot/DHML_PARDE DHML_PARDE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.  
[[https://www.uniprot.org/uniprot/CYCL_PARDE CYCL_PARDE]] Electron acceptor for MDH. Acts in methanol oxidation. [[https://www.uniprot.org/uniprot/DHMH_PARDE DHMH_PARDE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. [[https://www.uniprot.org/uniprot/AMCY_PARDE AMCY_PARDE]] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin. [[https://www.uniprot.org/uniprot/DHML_PARDE DHML_PARDE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mt/2mta_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mt/2mta_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2mta ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2mta" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cytochrome c|Cytochrome c]]
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
== References ==
== References ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Amine dehydrogenase]]
[[Category: Atcc 17741]]
[[Category: Paracoccus denitrificans]]
[[Category: Large Structures]]
[[Category: Chen, L]]
[[Category: Chen, L]]
[[Category: Mathews, F S]]
[[Category: Mathews, F S]]
[[Category: Electron transport]]
[[Category: Electron transport]]

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