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New page: left|200px<br /><applet load="1id2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1id2, resolution 2.15Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1id2.gif|left|200px]]<br /><applet load="1id2" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1id2, resolution 2.15&Aring;" />
'''CRYSTAL STRUCTURE OF AMICYANIN FROM PARACOCCUS VERSUTUS (THIOBACILLUS VERSUTUS)'''<br />


==Overview==
==CRYSTAL STRUCTURE OF AMICYANIN FROM PARACOCCUS VERSUTUS (THIOBACILLUS VERSUTUS)==
The crystal structure of the type I blue copper protein amicyanin from, Thiobacillus versutus has been determined by Patterson search techniques, on the basis of the molecular model of amicyanin from Paracoccus, denitrificans, and refined by energy-restrained least-squares methods., Amicyanin crystallizes in the trigonal space group P3(2) with unit cell, dimensions of a = b = 87.40 A, c = 38.20 A. The asymmetric unit is, composed of three independent molecules centred on the crystallographic, 3(2) axes. The final R-value is 17.4% for 15,984 reflections to a, resolution of 2.15 A. The polypeptide fold in amicyanin is based on the, beta-sandwich structure commonly found in blue copper proteins. Nine beta, strands are folded into two twisted beta-sheets that pack together with a, filling of non-polar residues between them. The geometry of the copper, site is similar to that of plastocyanin. There are four ligands, arranged, approximately as a distorted tetrahedron, to the copper atom: His54, Cys93, His96 and Met99. One of the copper ligands, His96, is exposed to, the surface and lies in the centre of a cluster of seven hydrophobic, residues.
<StructureSection load='1id2' size='340' side='right'caption='[[1id2]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1id2]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_versutus Paracoccus versutus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ID2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ID2 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]] 2.15&#8491;</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=1id2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1id2 OCA], [https://pdbe.org/1id2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1id2 RCSB], [https://www.ebi.ac.uk/pdbsum/1id2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1id2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMCY_PARVE AMCY_PARVE] Primary acceptor of electrons from methylamine dehydrogenase. Passes those electrons on either a soluble cytochrome c or to pseudoazurin.
== 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/id/1id2_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=1id2 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the type I blue copper protein amicyanin from Thiobacillus versutus has been determined by Patterson search techniques on the basis of the molecular model of amicyanin from Paracoccus denitrificans, and refined by energy-restrained least-squares methods. Amicyanin crystallizes in the trigonal space group P3(2) with unit cell dimensions of a = b = 87.40 A, c = 38.20 A. The asymmetric unit is composed of three independent molecules centred on the crystallographic 3(2) axes. The final R-value is 17.4% for 15,984 reflections to a resolution of 2.15 A. The polypeptide fold in amicyanin is based on the beta-sandwich structure commonly found in blue copper proteins. Nine beta strands are folded into two twisted beta-sheets that pack together with a filling of non-polar residues between them. The geometry of the copper site is similar to that of plastocyanin. There are four ligands, arranged approximately as a distorted tetrahedron, to the copper atom: His54, Cys93, His96 and Met99. One of the copper ligands, His96, is exposed to the surface and lies in the centre of a cluster of seven hydrophobic residues.


==About this Structure==
Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus.,Romero A, Nar H, Huber R, Messerschmidt A, Kalverda AP, Canters GW, Durley R, Mathews FS J Mol Biol. 1994 Mar 4;236(4):1196-211. PMID:8120896<ref>PMID:8120896</ref>
1ID2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_versutus Paracoccus versutus] 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=1ID2 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structure analysis and refinement at 2.15 A resolution of amicyanin, a type I blue copper protein, from Thiobacillus versutus., Romero A, Nar H, Huber R, Messerschmidt A, Kalverda AP, Canters GW, Durley R, Mathews FS, J Mol Biol. 1994 Mar 4;236(4):1196-211. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8120896 8120896]
</div>
<div class="pdbe-citations 1id2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Paracoccus versutus]]
[[Category: Paracoccus versutus]]
[[Category: Single protein]]
[[Category: Messerschmidt A]]
[[Category: Messerschmidt, A.]]
[[Category: Nar H]]
[[Category: Nar, H.]]
[[Category: Romero A]]
[[Category: Romero, A.]]
[[Category: CU]]
[[Category: beta barrel]]
[[Category: electron transfer protein]]
[[Category: type-1 blue copper protein]]
 
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Latest revision as of 08:05, 4 March 2026

CRYSTAL STRUCTURE OF AMICYANIN FROM PARACOCCUS VERSUTUS (THIOBACILLUS VERSUTUS)

1id2, resolution 2.15Å

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