View source for 2mta


==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=''>
== 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://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" 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='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://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>
== 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. 
== 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/mt/2mta_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=2mta ConSurf].
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== Publication Abstract from PubMed ==
The 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<ref>PMID:8140419</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Atcc 17741]]
[[Category: Large Structures]]
[[Category: Chen, L]]
[[Category: Mathews, F S]]
[[Category: Electron transport]]