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< | ==Crystal Structure of Cu(II)(Sal-Leu)/apo-Myoglobin== | ||
<StructureSection load='2eb9' size='340' side='right'caption='[[2eb9]], [[Resolution|resolution]] 1.80Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2eb9]] 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=2EB9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EB9 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]] 1.8Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CUS:(N-SALICYLIDEN-L-LEUCINATO)-COPPER(II)'>CUS</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2eb9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eb9 OCA], [https://pdbe.org/2eb9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eb9 RCSB], [https://www.ebi.ac.uk/pdbsum/2eb9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eb9 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/2eb9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2eb9 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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2eb9" style="background-color:#fffaf0;"></div> | |||
== | |||
==See Also== | ==See Also== | ||
*[[Myoglobin]] | *[[Myoglobin 3D structures|Myoglobin 3D structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Physeter catodon]] | [[Category: Physeter catodon]] | ||
[[Category: Abe | [[Category: Abe S]] | ||
[[Category: Hikage | [[Category: Hikage T]] | ||
[[Category: Okazaki | [[Category: Okazaki S]] | ||
[[Category: Suzuki | [[Category: Suzuki A]] | ||
[[Category: Ueno | [[Category: Ueno T]] | ||
[[Category: Watanabe | [[Category: Watanabe Y]] | ||
[[Category: Yamane | [[Category: Yamane T]] | ||
Latest revision as of 11:38, 25 October 2023
Crystal Structure of Cu(II)(Sal-Leu)/apo-MyoglobinCrystal Structure of Cu(II)(Sal-Leu)/apo-Myoglobin
Structural highlights
FunctionMYG_PHYMC Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedapo-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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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