1j2v: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(13 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1j2v.jpg|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1j2v", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_1j2v|  PDB=1j2v  |  SCENE=  }}
'''Crystal Structure of CutA1 from Pyrococcus Horikoshii'''


==Crystal Structure of CutA1 from Pyrococcus Horikoshii==
<StructureSection load='1j2v' size='340' side='right'caption='[[1j2v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1j2v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1J2V 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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1j2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j2v OCA], [https://pdbe.org/1j2v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1j2v RCSB], [https://www.ebi.ac.uk/pdbsum/1j2v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1j2v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CUTA_PYRHO CUTA_PYRHO] Involved in resistance toward heavy metals.
== 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/j2/1j2v_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=1j2v ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
CutA is a small protein that appears to be involved in the mechanism of divalent metal cation tolerance in microorganisms. Here we report the crystal structure of Pyrococcus horikoshii CutA (PhoCutA), with and without Cu(2+), and its metal-binding properties. Crystallographic analyses revealed that PhoCutA forms a stable trimeric structure with intertwined antiparallel beta-strands. The crystal structure of the Cu(2+)-PhoCutA complex shows that the Cu(2+) is located at a trimer-trimer interface and is recognized by the side chains of one Asp(48) from each trimer. In an in vitro experiment, PhoCutA bound to several heavy metals, most of which led to reversible aggregation of the protein; i.e. the aggregates could be completely solubilized by addition of ethylenediamine tetraacetic acid (EDTA) or dialysis against metal free buffer. Substitution of Asp(48) with Ala led to a decrease in the amount of aggregates, suggesting the significant contribution of Asp(48) to the reversible aggregation. To the best of our knowledge, this is the first report which provides the structural evidence for heavy metal-induced multimerization of a protein.


==Overview==
Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA.,Tanaka Y, Tsumoto K, Nakanishi T, Yasutake Y, Sakai N, Yao M, Tanaka I, Kumagai I FEBS Lett. 2004 Jan 2;556(1-3):167-74. PMID:14706845<ref>PMID:14706845</ref>
CutA is a small protein that appears to be involved in the mechanism of divalent metal cation tolerance in microorganisms. Here we report the crystal structure of Pyrococcus horikoshii CutA (PhoCutA), with and without Cu(2+), and its metal-binding properties. Crystallographic analyses revealed that PhoCutA forms a stable trimeric structure with intertwined antiparallel beta-strands. The crystal structure of the Cu(2+)-PhoCutA complex shows that the Cu(2+) is located at a trimer-trimer interface and is recognized by the side chains of one Asp(48) from each trimer. In an in vitro experiment, PhoCutA bound to several heavy metals, most of which led to reversible aggregation of the protein; i.e. the aggregates could be completely solubilized by addition of ethylenediamine tetraacetic acid (EDTA) or dialysis against metal free buffer. Substitution of Asp(48) with Ala led to a decrease in the amount of aggregates, suggesting the significant contribution of Asp(48) to the reversible aggregation. To the best of our knowledge, this is the first report which provides the structural evidence for heavy metal-induced multimerization of a protein.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1J2V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J2V OCA].
</div>
<div class="pdbe-citations 1j2v" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Structural implications for heavy metal-induced reversible assembly and aggregation of a protein: the case of Pyrococcus horikoshii CutA., Tanaka Y, Tsumoto K, Nakanishi T, Yasutake Y, Sakai N, Yao M, Tanaka I, Kumagai I, FEBS Lett. 2004 Jan 2;556(1-3):167-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14706845 14706845]
*[[CutA1 3D structures|CutA1 3D structures]]
[[Category: Pyrococcus horikoshii]]
== References ==
[[Category: Single protein]]
<references/>
[[Category: Kumagai, I.]]
__TOC__
[[Category: Sakai, N.]]
</StructureSection>
[[Category: Tanaka, I.]]
[[Category: Large Structures]]
[[Category: Tanaka, Y.]]
[[Category: Pyrococcus horikoshii OT3]]
[[Category: Tsumoto, K.]]
[[Category: Kumagai I]]
[[Category: Yao, M.]]
[[Category: Sakai N]]
[[Category: Yasutake, Y.]]
[[Category: Tanaka I]]
[[Category: Alpha + beta]]
[[Category: Tanaka Y]]
[[Category: Structural genomic]]
[[Category: Tsumoto K]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 20:44:11 2008''
[[Category: Yao M]]
[[Category: Yasutake Y]]

Latest revision as of 06:47, 30 October 2024

Crystal Structure of CutA1 from Pyrococcus Horikoshii

1j2v, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA