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[[Image:2eb8.jpg|left|200px]]
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{{STRUCTURE_2eb8|  PDB=2eb8  |  SCENE=  }}
'''Crystal Structure of Cu(II)(Sal-Phe)/apo-Myoglobin'''


==Crystal Structure of Cu(II)(Sal-Phe)/apo-Myoglobin==
<StructureSection load='2eb8' size='340' side='right'caption='[[2eb8]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2eb8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EB8 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]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CUP:(N-SALICYLIDEN-L-PHENYLALANATO)-COPPER(II)'>CUP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=2eb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eb8 OCA], [https://pdbe.org/2eb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eb8 RCSB], [https://www.ebi.ac.uk/pdbsum/2eb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eb8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
== 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/eb/2eb8_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=2eb8 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
apo-Myoglobin (apo-Mb) was reconstituted with three copper complexes: CuII(Sal-Phe) (1; Sal-Phe = N-salicylidene-L-phenylalanato), CuII(Sal-Leu) (2; Sal-Leu = N-salicylidene-L-leucinato), and CuII(Sal-Ala) (3; Sal-Ala = N-salicylidene-L-alanato). The crystal structures of 1.apo-Mb (1.65 Angstrom resolution) and 2.apo-Mb (1.8 Angstrom resolution) show that the coordination geometry around the CuII atom in apo-Mb is distorted square-planar with tridentate Sal-X and a Nepsilon atom of His64 in the apo-Mb cavity and the plane of these copper complexes is perpendicular to that of heme. These results suggest that the apo-Mb cavity can hold metal complexes with various coordination geometries.


==Overview==
Design and structure analysis of artificial metalloproteins: selective coordination of His64 to copper complexes with square-planar structure in the apo-myoglobin scaffold.,Abe S, Ueno T, Reddy PA, Okazaki S, Hikage T, Suzuki A, Yamane T, Nakajima H, Watanabe Y Inorg Chem. 2007 Jun 25;46(13):5137-9. Epub 2007 May 25. PMID:17523632<ref>PMID:17523632</ref>
apo-Myoglobin (apo-Mb) was reconstituted with three copper complexes: CuII(Sal-Phe) (1; Sal-Phe = N-salicylidene-L-phenylalanato), CuII(Sal-Leu) (2; Sal-Leu = N-salicylidene-L-leucinato), and CuII(Sal-Ala) (3; Sal-Ala = N-salicylidene-L-alanato). The crystal structures of 1.apo-Mb (1.65 Angstrom resolution) and 2.apo-Mb (1.8 Angstrom resolution) show that the coordination geometry around the CuII atom in apo-Mb is distorted square-planar with tridentate Sal-X and a Nepsilon atom of His64 in the apo-Mb cavity and the plane of these copper complexes is perpendicular to that of heme. These results suggest that the apo-Mb cavity can hold metal complexes with various coordination geometries.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2EB8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EB8 OCA].
</div>
<div class="pdbe-citations 2eb8" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Design and structure analysis of artificial metalloproteins: selective coordination of His64 to copper complexes with square-planar structure in the apo-myoglobin scaffold., Abe S, Ueno T, Reddy PA, Okazaki S, Hikage T, Suzuki A, Yamane T, Nakajima H, Watanabe Y, Inorg Chem. 2007 Jun 25;46(13):5137-9. Epub 2007 May 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17523632 17523632]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
[[Category: Single protein]]
[[Category: Abe S]]
[[Category: Abe, S.]]
[[Category: Hikage T]]
[[Category: Hikage, T.]]
[[Category: Okazaki S]]
[[Category: Okazaki, S.]]
[[Category: Suzuki A]]
[[Category: Suzuki, A.]]
[[Category: Ueno T]]
[[Category: Ueno, T.]]
[[Category: Watanabe Y]]
[[Category: Watanabe, Y.]]
[[Category: Yamane T]]
[[Category: Yamane, T.]]
[[Category: Oxygen storage/transport]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 02:16:13 2008''

Latest revision as of 07:57, 13 August 2026

Crystal Structure of Cu(II)(Sal-Phe)/apo-Myoglobin

2eb8, resolution 1.65Å

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