1nz4

<StructureSection load='1nz4' size='340' side='right' caption='[[1nz4]], [[Resolution|resolution]] 1.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1nz4]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NZ4 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1wla|1wla]], [[1nz2|1nz2]], [[1nz3|1nz3]], [[1nz5|1nz5]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9796 Equus caballus])</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=1nz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nz4 OCA], [http://pdbe.org/1nz4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nz4 RCSB], [http://www.ebi.ac.uk/pdbsum/1nz4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nz4 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nz/1nz4_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

 

== References ==

[[Category: Brayer, G D]]

[[Category: Hunter, C L]]

[[Category: Lee, H]]

[[Category: Mauk, A G]]

[[Category: Mauk, M R]]

[[Category: Maurus, R]]

[[Category: Nguyen, N]]

[[Category: Raven, E L]]

[[Category: Smith, S]]

[[Category: Tong, H]]

[[Category: Oxygen storage-transport complex]]