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1cuo

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(New page: 200px<br /><applet load="1cuo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cuo, resolution 1.60&Aring;" /> '''CRYSTAL STRUCTURE AN...)
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[[Image:1cuo.jpg|left|200px]]<br /><applet load="1cuo" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cuo, resolution 1.60&Aring;" />
 
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'''CRYSTAL STRUCTURE ANALYSIS OF ISOMER-2 AZURIN FROM METHYLOMONAS J'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE ANALYSIS OF ISOMER-2 AZURIN FROM METHYLOMONAS J==
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The obligate methylotroph Methylomonas sp. strain J produces two azurins, (Az-iso1 and Az-iso2) as candidates for electron acceptor from methylamine, dehydrogenase (MADH) in the electron-transfer process involving the, oxidation of methylamine to formaldehyde and ammonia. The X-ray, crystallographic study indicated that Az-iso2 gives two types of crystals, (form I and form II) with polyethylene glycol (PEG4000) and ammonium, sulfate as the precipitants, respectively. Comparison between the two, Az-iso2 structures in forms I and II reveals the remarkable structural, changes at the top surface of the molecule around the copper atom. Az-iso2, possesses Gly43 instead of Val43 or Ala43, which is unique among all other, azurins around the copper ligand His46, inducing the remarkable structural, change in the loop region from Gly37 to Gly43. When the structure of, Az-iso2 is superimposed on that of amicyanin in the ternary complex, composed of MADH, amicyanin, and cytochrome c(551), the loop of Az-iso2, deeply overlaps with the light subunit of MADH. However, the Az-iso2, molecule is probably able to avoid any steric hindrance with the cognate, MADH to form the complex for intermolecular electron-transfer reaction, since the loop containing Gly43 is flexible. We discuss why the, electron-transfer activity of Az-iso2 is fivefold higher than that of, Az-iso1.
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<StructureSection load='1cuo' size='340' side='right'caption='[[1cuo]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cuo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylomonas_sp._J Methylomonas sp. J]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CUO FirstGlance]. <br>
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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]] 1.6&#8491;</td></tr>
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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></td></tr>
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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=1cuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cuo OCA], [https://pdbe.org/1cuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cuo RCSB], [https://www.ebi.ac.uk/pdbsum/1cuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cuo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AZUR2_METJ AZUR2_METJ] This methylothroph organism uses azurin in the oxidation of methylamine. Iso-2 is probably the acceptor of electrons from methylamine dehydrogenase.
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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/cu/1cuo_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=1cuo ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1CUO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methylomonas_sp._j Methylomonas sp. j] with CU as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CUO OCA].
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*[[Azurin 3D structures|Azurin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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The significance of the flexible loop in the azurin (Az-iso2) from the obligate methylotroph Methylomonas sp. strain J., Inoue T, Suzuki S, Nishio N, Yamaguchi K, Kataoka K, Tobari J, Yong X, Hamanaka S, Matsumura H, Kai Y, J Mol Biol. 2003 Oct 10;333(1):117-24. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14516747 14516747]
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[[Category: Large Structures]]
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[[Category: Methylomonas sp. j]]
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[[Category: Methylomonas sp. J]]
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[[Category: Single protein]]
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[[Category: Inoue T]]
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[[Category: Inoue, T.]]
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[[Category: Kai Y]]
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[[Category: Kai, Y.]]
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[[Category: Kataoka K]]
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[[Category: Kataoka, K.]]
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[[Category: Nishio N]]
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[[Category: Nishio, N.]]
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[[Category: Suzuki S]]
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[[Category: Suzuki, S.]]
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[[Category: CU]]
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[[Category: beta barrel]]
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[[Category: electron transport]]
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[[Category: periplasmic]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:46:20 2007''
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Current revision

CRYSTAL STRUCTURE ANALYSIS OF ISOMER-2 AZURIN FROM METHYLOMONAS J

PDB ID 1cuo

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