2frf: Difference between revisions

No edit summary
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2frf.png|left|200px]]


<!--
==Horse Heart Myoglobin, Nitrite Adduct, Crystal Soak==
The line below this paragraph, containing "STRUCTURE_2frf", creates the "Structure Box" on the page.
<StructureSection load='2frf' size='340' side='right'caption='[[2frf]], [[Resolution|resolution]] 1.20&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'>[[2frf]] 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=2FRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FRF 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]] 1.2&#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=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
{{STRUCTURE_2frf|  PDB=2frf  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2frf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2frf OCA], [https://pdbe.org/2frf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2frf RCSB], [https://www.ebi.ac.uk/pdbsum/2frf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2frf 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/fr/2frf_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=2frf ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nitrite is an important species in the global nitrogen cycle, and the nitrite reductase enzymes convert nitrite to nitric oxide (NO). Recently, it has been shown that hemoglobin and myoglobin catalyze the reduction of nitrite to NO under hypoxic conditions. We have determined the 1.20 A resolution crystal structure of the nitrite adduct of ferric horse heart myoglobin (hh Mb). The ligand is bound to iron in the nitrito form, and the complex is formulated as MbIII(ONO-). The Fe-ONO bond length is 1.94 A, and the O-N-O angle is 113 degrees . In addition, the nitrite ligand is stabilized by hydrogen bonding with the distal His64 residue. We have also determined the 1.30 A resolution crystal structures of hh MbIINO. When hh MbIINO is prepared from the reaction of metMbIII with nitrite/dithionite, the FeNO angle is 144 degrees with a Fe-NO bond length of 1.87 A. However, when prepared from the reaction of NO with reduced MbII, the FeNO angle is 120 degrees with a Fe-NO bond length of 2.13 A. This difference in FeNO conformations as a function of preparative method is reproducible, and suggests a role of the distal pocket in hh MbIINO in stabilizing local FeNO conformational minima.


===Horse Heart Myoglobin, Nitrite Adduct, Crystal Soak===
Crystal structures of the nitrite and nitric oxide complexes of horse heart myoglobin.,Copeland DM, Soares AS, West AH, Richter-Addo GB J Inorg Biochem. 2006 Aug;100(8):1413-25. Epub 2006 May 5. PMID:16777231<ref>PMID:16777231</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_16777231}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2frf" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 16777231 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_16777231}}
 
==About this Structure==
[[2frf]] 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=2FRF OCA].


==See Also==
==See Also==
*[[Myoglobin]]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:16777231</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Copeland, D M.]]
[[Category: Large Structures]]
[[Category: Richter-Addo, G B.]]
[[Category: Copeland DM]]
[[Category: Soares, A S.]]
[[Category: Richter-Addo GB]]
[[Category: West, A H.]]
[[Category: Soares AS]]
[[Category: Heme]]
[[Category: West AH]]
[[Category: Iron]]
[[Category: Myoglobin]]
[[Category: Nitric oxide]]
[[Category: Nitrite]]
[[Category: No]]
[[Category: No2]]
[[Category: Oxygen storage/transport complex]]

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

OCA