2cmm: Difference between revisions

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[[Image:2cmm.png|left|200px]]


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==STRUCTURAL ANALYSIS OF THE MYOGLOBIN RECONSTITUTED WITH IRON PORPHINE==
The line below this paragraph, containing "STRUCTURE_2cmm", creates the "Structure Box" on the page.
<StructureSection load='2cmm' size='340' side='right'caption='[[2cmm]], [[Resolution|resolution]] 1.80&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'>[[2cmm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CMM 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]] 1.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYN:CYANIDE+ION'>CYN</scene></td></tr>
{{STRUCTURE_2cmm|  PDB=2cmm  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2cmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cmm OCA], [https://pdbe.org/2cmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cmm RCSB], [https://www.ebi.ac.uk/pdbsum/2cmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cmm ProSAT]</span></td></tr>
</table>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cm/2cmm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2cmm ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sperm whale apomyoglobin was complexed with iron porphine to examine the influence of completely removed heme side chains on the entire molecular structure. Paramagnetic NMR peak from the proximal histidine of the deoxy protein ensured formation of the iron-histidine bond. Porphine pyrrole-proton NMR signals of the cyanmet and deoxy derivatives are unusually sharp single lines manifesting rapid heme rotation about the iron-histidine bond. X-ray crystallographic structure of the cyanmet derivative, determined with a final R factor of 0.21 for 11,808 independent reflections ranging from 7 to 1.8 A, was resolved at 1.8 A resolution. The result confirmed 1:1 coupling between apomyoglobin and iron porphine. The cyano ligand adopts a bent configuration with an Fe-C-N angle of 127 degrees and a Fe-CN distance of 1.89 A. The overall globin structure and side chain conformations are remarkably similar to those of native myoglobin despite intensive disruption of the original heme-globin interactions. The native apoprotein structure unexpectedly conserved even after iron porphine insertion demonstrates that the complex polypeptide fold of holomyoglobin is more inherent in the amino acid sequence than is generally believed.


===STRUCTURAL ANALYSIS OF THE MYOGLOBIN RECONSTITUTED WITH IRON PORPHINE===
Structural analysis of the myoglobin reconstituted with iron porphine.,Neya S, Funasaki N, Sato T, Igarashi N, Tanaka N J Biol Chem. 1993 Apr 25;268(12):8935-42. PMID:8473336<ref>PMID:8473336</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2cmm" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_8473336}}, adds the Publication Abstract to the page
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 8473336 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_8473336}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2CMM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CMM OCA].
 
==Reference==
Structural analysis of the myoglobin reconstituted with iron porphine., Neya S, Funasaki N, Sato T, Igarashi N, Tanaka N, J Biol Chem. 1993 Apr 25;268(12):8935-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8473336 8473336]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
[[Category: Single protein]]
[[Category: Funasaki N]]
[[Category: Funasaki, N.]]
[[Category: Igarashi N]]
[[Category: Igarashi, N.]]
[[Category: Iizuka T]]
[[Category: Iizuka, T.]]
[[Category: Moriyama H]]
[[Category: Moriyama, H.]]
[[Category: Neya S]]
[[Category: Neya, S.]]
[[Category: Sato T]]
[[Category: Sato, T.]]
[[Category: Shiro Y]]
[[Category: Shiro, Y.]]
[[Category: Tanaka N]]
[[Category: Tanaka, N.]]
[[Category: Oxygen transport]]
 
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Retrieved from "https://proteopedia.org/2cmm"