1cuo: Difference between revisions
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New page: left|200px<br /><applet load="1cuo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cuo, resolution 1.60Å" /> '''CRYSTAL STRUCTURE AN... |
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== | ==CRYSTAL STRUCTURE ANALYSIS OF ISOMER-2 AZURIN FROM METHYLOMONAS J== | ||
The obligate methylotroph Methylomonas sp. strain J produces two azurins | <StructureSection load='1cuo' size='340' side='right'caption='[[1cuo]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | |||
<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> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</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></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=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> | |||
</table> | |||
== Function == | |||
[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. | |||
== 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/cu/1cuo_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1cuo ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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:14516747<ref>PMID:14516747</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cuo" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Azurin 3D structures|Azurin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Methylomonas sp. J]] | |||
[[Category: Inoue T]] | |||
[[Category: Kai Y]] | |||
[[Category: Kataoka K]] | |||
[[Category: Nishio N]] | |||
[[Category: Suzuki S]] | |||
Latest revision as of 04:26, 17 October 2024
CRYSTAL STRUCTURE ANALYSIS OF ISOMER-2 AZURIN FROM METHYLOMONAS J
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