1nz2: Difference between revisions

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-[[Image:1nz2.png|left|200px]]
-<!--
+==K45E Variant of Horse Heart Myoglobin==
-The line below this paragraph, containing "STRUCTURE_1nz2", creates the "Structure Box" on the page.
+<StructureSection load='1nz2' size='340' side='right'caption='[[1nz2]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1nz2]] 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=1NZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NZ2 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_1nz2|  PDB=1nz2  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nz2 OCA], [https://pdbe.org/1nz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nz2 RCSB], [https://www.ebi.ac.uk/pdbsum/1nz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nz2 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/1nz2_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=1nz2 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== 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.
-===K45E Variant of Horse Heart Myoglobin===
+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:12644706<ref>PMID:12644706</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_12644706}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1nz2" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 12644706 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_12644706}}
-==About this Structure==
-[[1nz2]] is a 1 chain structure of [[Myoglobin]] 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=1NZ2 OCA].
 ==See Also==
-*[[Myoglobin]]
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:12644706</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Equus caballus]]
-[[Category: Brayer, G D.]]
+[[Category: Large Structures]]
-[[Category: Hunter, C L.]]
+[[Category: Brayer GD]]
-[[Category: Lee, H.]]
+[[Category: Hunter CL]]
-[[Category: Mauk, A G.]]
+[[Category: Lee H]]
-[[Category: Mauk, M R.]]
+[[Category: Mauk AG]]
-[[Category: Maurus, R.]]
+[[Category: Mauk MR]]
-[[Category: Nguyen, N.]]
+[[Category: Maurus R]]
-[[Category: Raven, E L.]]
+[[Category: Nguyen N]]
-[[Category: Smith, M.]]
+[[Category: Raven EL]]
-[[Category: Tong, H.]]
+[[Category: Smith M]]
-[[Category: Heme]]
+[[Category: Tong H]]
-[[Category: Muscle]]
-[[Category: Oxygen storage/transport complex]]
-[[Category: Oxygen transport]]