2eb8

From Proteopedia

(Difference between revisions)

Revision as of 17:22, 15 December 2021

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

Structural highlights

2eb8 is a 1 chain structure with sequence from Phycd. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	2eb9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MYG_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 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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Abe S, Ueno T, Reddy PA, Okazaki S, Hikage T, Suzuki A, Yamane T, Nakajima H, Watanabe Y. Design and structure analysis of artificial metalloproteins: selective coordination of His64 to copper complexes with square-planar structure in the apo-myoglobin scaffold. Inorg Chem. 2007 Jun 25;46(13):5137-9. Epub 2007 May 25. PMID:17523632 doi:10.1021/ic070289m

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2eb8"

@@ Line 3: / Line 3: @@
 <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 [http://en.wikipedia.org/wiki/Phycd Phycd]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EB8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2eb8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phycd Phycd]. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CUP:(N-SALICYLIDEN-L-PHENYLALANATO)-COPPER(II)'>CUP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2eb9|2eb9]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2eb9|2eb9]]</div></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eb8 OCA], [http://pdbe.org/2eb8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eb8 RCSB], [http://www.ebi.ac.uk/pdbsum/2eb8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2eb8 ProSAT]</span></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 ==
-[[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+[[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]]

2eb8

From Proteopedia

Revision as of 17:22, 15 December 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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