1nz4: Difference between revisions

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New page: left|200px<br /><applet load="1nz4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nz4, resolution 1.8Å" /> '''The horse heart myogl...
 
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[[Image:1nz4.jpg|left|200px]]<br /><applet load="1nz4" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1nz4, resolution 1.8&Aring;" />
'''The horse heart myoglobin variant K45E/K63E complexed with Cadmium'''<br />


==Overview==
==The horse heart myoglobin variant K45E/K63E complexed with Cadmium==
A binding site for metal ions has been created on the surface of horse, heart myoglobin (Mb) near the heme 6-propionate group by replacing K45 and, K63 with glutamyl residues. One-dimensional (1)H NMR spectroscopy, indicates that Mn(2+) binds in the vicinity of the heme 6-propionate as, anticipated, and potentiometric titrations establish that the affinity of, the new site for Mn(2+) is 1.28(4) x 10(4) M(-1) (pH 6.96, ionic strength, I = 17.2 microM, 25 degrees C). In addition, these substitutions lower the, reduction potential of the protein and increase the pK(a) for the water, molecule coordinated to the heme iron of metmyoglobin. The peroxidase, [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid), ABTS, as substrate], and the Mn(2+)-peroxidase activity of the variant are both increased, approximately 3-fold. In contrast to wild-type Mb, both the affinity for, azide and the midpoint potential of the variant are significantly, influenced by the addition of Mn(2+). The structure of the variant has, been determined by x-ray crystallography to define the coordination, environment of bound Mn(2+) and Cd(2+). Although slight differences are, observed between the geometry of the binding of the two metal ions, both, are hexacoordinate, and neither involves coordination by E63.
<StructureSection load='1nz4' size='340' side='right'caption='[[1nz4]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1nz4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NZ4 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1nz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nz4 OCA], [https://pdbe.org/1nz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nz4 RCSB], [https://www.ebi.ac.uk/pdbsum/1nz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nz4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] 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/nz/1nz4_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=1nz4 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1NZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with CD and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NZ4 OCA].
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Introduction and characterization of a functionally linked metal ion binding site at the exposed heme edge of myoglobin., Hunter CL, Maurus R, Mauk MR, Lee H, Raven EL, Tong H, Nguyen N, Smith M, Brayer GD, Mauk AG, Proc Natl Acad Sci U S A. 2003 Apr 1;100(7):3647-52. Epub 2003 Mar 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12644706 12644706]
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brayer, G.D.]]
[[Category: Brayer GD]]
[[Category: Hunter, C.L.]]
[[Category: Hunter CL]]
[[Category: Lee, H.]]
[[Category: Lee H]]
[[Category: Mauk, A.G.]]
[[Category: Mauk AG]]
[[Category: Mauk, M.R.]]
[[Category: Mauk MR]]
[[Category: Maurus, R.]]
[[Category: Maurus R]]
[[Category: Nguyen, N.]]
[[Category: Nguyen N]]
[[Category: Raven, E.L.]]
[[Category: Raven EL]]
[[Category: Smith, S.]]
[[Category: Smith S]]
[[Category: Tong, H.]]
[[Category: Tong H]]
[[Category: CD]]
[[Category: HEM]]
[[Category: cadmium cd2+ horse heart myoglobin engineered metal binding site]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:40:37 2007''

Latest revision as of 11:00, 14 February 2024

The horse heart myoglobin variant K45E/K63E complexed with CadmiumThe horse heart myoglobin variant K45E/K63E complexed with Cadmium

Structural highlights

1nz4 is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYG_HORSE 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.

See Also

1nz4, resolution 1.80Å

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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