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2gc4

From Proteopedia

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[[Image:2gc4.gif|left|200px]]
 
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{{Structure
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==Structural comparison of the oxidized ternary electron transfer complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans with the substrate-reduced, copper free complex at 1.9 A resolution.==
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|PDB= 2gc4 |SIZE=350|CAPTION= <scene name='initialview01'>2gc4</scene>, resolution 1.90&Aring;
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<StructureSection load='2gc4' size='340' side='right'caption='[[2gc4]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
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<table><tr><td colspan='2'>[[2gc4]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GC4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GC4 FirstGlance]. <br>
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|ACTIVITY= [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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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|GENE=
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<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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gc4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gc4 OCA], [https://pdbe.org/2gc4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gc4 RCSB], [https://www.ebi.ac.uk/pdbsum/2gc4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gc4 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gc/2gc4_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2gc4 ConSurf].
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<div style="clear:both"></div>
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'''Structural comparison of the oxidized ternary electron transfer complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans with the substrate-reduced, copper free complex at 1.9 A resolution.'''
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==See Also==
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*[[Amicyanin 3D structures|Amicyanin 3D structures]]
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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==Overview==
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*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
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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.
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2GC4 is a [[Protein complex]] structure of sequences 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=2GC4 OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/8140419 8140419]
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[[Category: Amine dehydrogenase]]
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[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
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[[Category: Protein complex]]
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[[Category: Chen Z]]
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[[Category: Chen, Z.]]
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[[Category: Davidson VL]]
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[[Category: Davidson, V L.]]
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[[Category: Durley R]]
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[[Category: Durley, R.]]
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[[Category: Mathews FS]]
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[[Category: Mathews, F S.]]
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[[Category: CU]]
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[[Category: HEM]]
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[[Category: NA]]
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[[Category: blue copper protein]]
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[[Category: cytochrome]]
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[[Category: electron transfer]]
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[[Category: methylamine dehydrogenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:02:57 2008''
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Current revision

Structural comparison of the oxidized ternary electron transfer complex of methylamine dehydrogenase, amicyanin and cytochrome c551i from Paracoccus denitrificans with the substrate-reduced, copper free complex at 1.9 A resolution.

PDB ID 2gc4

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