View source for 1ufj

==Crystal Structure of an Artificial Metalloprotein:Fe(III)(3,3'-Me2-salophen)/apo-A71G Myoglobin==
<StructureSection load='1ufj' size='340' side='right' caption='[[1ufj]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ufj]] 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=1UFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UFJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CZM:N,N-BIS-(2-HYDROXY-3-METHYL-BENZYLIDENE)-BENZENE-1,2-DIAMINE'>CZM</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ufj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ufj OCA], [http://pdbe.org/1ufj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ufj RCSB], [http://www.ebi.ac.uk/pdbsum/1ufj PDBsum]</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. 
== 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/uf/1ufj_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=1ufj ConSurf].
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== Publication Abstract from PubMed ==
Apo-myoglobin (apo-Mb) and apo-A71GMb were successfully reconstituted with FeIII(salophen) (1) (salophen = N,N'-bis(salicylidene)-1,2-phenilenediamine), Fe(III)(3,3'-Me2-salophen) (2), and FeIII(5,5'-t-Bu2-salophen) (3). The crystal structure of 2.apo-A71GMb shows the tight binding of the complex in the Mb cavity, while in wild-type apo-Mb it is highly disordered due to the steric repulsion with Ala71. Furthermore, the structure of 2.apo-A71GMb suggests a possible accommodation of a small substrate in the cavity. In fact, the cyanide association rate constant of 2.apo-A71GMb is 216-fold larger compared to that of 2.apo-Mb. These results provide us principles for the noncovalent fixation of synthetic metal cofactors at the desired positions in protein matrixes.

Crystal structures of artificial metalloproteins: tight binding of FeIII(Schiff-Base) by mutation of Ala71 to Gly in apo-myoglobin.,Ueno T, Ohashi M, Kono M, Kondo K, Suzuki A, Yamane T, Watanabe Y Inorg Chem. 2004 May 3;43(9):2852-8. PMID:15106972<ref>PMID:15106972</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1ufj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Myoglobin|Myoglobin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Phycd]]
[[Category: Kondo, K]]
[[Category: Kono, M]]
[[Category: Ohashi, M]]
[[Category: Suzuki, A]]
[[Category: Ueno, T]]
[[Category: Watanabe, Y]]
[[Category: Yamane, T]]
[[Category: Iron]]
[[Category: Metalloprotein]]
[[Category: Myoglobin]]
[[Category: Oxygen storage-transport complex]]
[[Category: Salophen]]
[[Category: Schiff base]]