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[[Image:2o5o.gif|left|200px]]<br /><applet load="2o5o" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2o5o, resolution 1.60&Aring;" />
'''Manganese horse heart myoglobin, nitrite modified'''<br />


==Overview==
==Manganese horse heart myoglobin, nitrite modified==
Nitrite is now recognized as a storage pool of bioactive nitric oxide, (NO). Hemoglobin (Hb) and myoglobin (Mb) convert, under certain, conditions, nitrite to NO. This newly discovered nitrite reductase, activity of Hb and Mb provides an attractive alternative to mammalian NO, synthesis from the NO synthase pathway that requires dioxygen. We recently, reported the X-ray crystal structure of the nitrite adduct of ferric horse, heart Mb, and showed that the nitrite ligand binds in an unprecedented, O-binding (nitrito) mode to the d(5) ferric center in Mb(III)(ONO) [D.M., Copeland, A. Soares, A.H. West, G.B. Richter-Addo, J. Inorg. Biochem. 100, (2006) 1413-1425]. We also showed that the distal pocket in Mb allows for, different conformations of the NO ligand (120 degrees and 144 degrees ) in, Mb(II)NO depending on the mode of preparation of the compound. In this, article, we report the crystal structures of the nitrite and NO adducts of, manganese-substituted hh Mb (a d(4) system) and of the nitrite adduct of, cobalt-substituted hh Mb (a d(6) system). We show that the distal His64, residue directs the nitrite ligand towards the rare nitrito O-binding mode, in Mn(III)Mb and Co(III)Mb. We also report that the distal pocket residues, allow a stabilization of an unprecendented bent MnNO moiety in Mn(II)MbNO., These crystal structural data, when combined with the data for the aquo, methanol, and azide MnMb derivatives, provide information on the role of, distal pocket residues in the observed binding modes of nitrite and NO, ligands to wild-type and metal-substituted Mb.
<StructureSection load='2o5o' size='340' side='right'caption='[[2o5o]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2o5o]] 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=2O5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2O5O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MNR:PROTOPORPHYRIN+IX+CONTAINING+MN'>MNR</scene>, <scene name='pdbligand=NO2:NITRITE+ION'>NO2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2o5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2o5o OCA], [https://pdbe.org/2o5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2o5o RCSB], [https://www.ebi.ac.uk/pdbsum/2o5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2o5o 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/o5/2o5o_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=2o5o ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nitrite is now recognized as a storage pool of bioactive nitric oxide (NO). Hemoglobin (Hb) and myoglobin (Mb) convert, under certain conditions, nitrite to NO. This newly discovered nitrite reductase activity of Hb and Mb provides an attractive alternative to mammalian NO synthesis from the NO synthase pathway that requires dioxygen. We recently reported the X-ray crystal structure of the nitrite adduct of ferric horse heart Mb, and showed that the nitrite ligand binds in an unprecedented O-binding (nitrito) mode to the d(5) ferric center in Mb(III)(ONO) [D.M. Copeland, A. Soares, A.H. West, G.B. Richter-Addo, J. Inorg. Biochem. 100 (2006) 1413-1425]. We also showed that the distal pocket in Mb allows for different conformations of the NO ligand (120 degrees and 144 degrees ) in Mb(II)NO depending on the mode of preparation of the compound. In this article, we report the crystal structures of the nitrite and NO adducts of manganese-substituted hh Mb (a d(4) system) and of the nitrite adduct of cobalt-substituted hh Mb (a d(6) system). We show that the distal His64 residue directs the nitrite ligand towards the rare nitrito O-binding mode in Mn(III)Mb and Co(III)Mb. We also report that the distal pocket residues allow a stabilization of an unprecendented bent MnNO moiety in Mn(II)MbNO. These crystal structural data, when combined with the data for the aquo, methanol, and azide MnMb derivatives, provide information on the role of distal pocket residues in the observed binding modes of nitrite and NO ligands to wild-type and metal-substituted Mb.


==About this Structure==
Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations.,Zahran ZN, Chooback L, Copeland DM, West AH, Richter-Addo GB J Inorg Biochem. 2008 Feb;102(2):216-33. Epub 2007 Aug 25. PMID:17905436<ref>PMID:17905436</ref>
2O5O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=NO2:'>NO2</scene> and <scene name='pdbligand=MNR:'>MNR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+X+157'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+X+158'>AC2</scene>, <scene name='pdbsite=AC3:No2+Binding+Site+For+Residue+X+159'>AC3</scene> and <scene name='pdbsite=AC4:Mnr+Binding+Site+For+Residue+X+154'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2O5O OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations., Zahran ZN, Chooback L, Copeland DM, West AH, Richter-Addo GB, J Inorg Biochem. 2007 Aug 25;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17905436 17905436]
</div>
<div class="pdbe-citations 2o5o" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Chooback, L.]]
[[Category: Chooback L]]
[[Category: Copeland, D.M.]]
[[Category: Copeland DM]]
[[Category: Richter-Addo, G.B.]]
[[Category: Richter-Addo GB]]
[[Category: West, A.H.]]
[[Category: West AH]]
[[Category: Zahran, Z.N.]]
[[Category: Zahran ZN]]
[[Category: MNR]]
[[Category: NO2]]
[[Category: SO4]]
[[Category: horse heart]]
[[Category: manganese myoglobin]]
[[Category: manganese protoporphyrin ix]]
[[Category: nitrite]]
[[Category: oxygen storage/transport complex]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:13:07 2008''

Latest revision as of 03:14, 28 December 2023

Manganese horse heart myoglobin, nitrite modifiedManganese horse heart myoglobin, nitrite modified

Structural highlights

2o5o is a 1 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYG_HORSE Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Nitrite is now recognized as a storage pool of bioactive nitric oxide (NO). Hemoglobin (Hb) and myoglobin (Mb) convert, under certain conditions, nitrite to NO. This newly discovered nitrite reductase activity of Hb and Mb provides an attractive alternative to mammalian NO synthesis from the NO synthase pathway that requires dioxygen. We recently reported the X-ray crystal structure of the nitrite adduct of ferric horse heart Mb, and showed that the nitrite ligand binds in an unprecedented O-binding (nitrito) mode to the d(5) ferric center in Mb(III)(ONO) [D.M. Copeland, A. Soares, A.H. West, G.B. Richter-Addo, J. Inorg. Biochem. 100 (2006) 1413-1425]. We also showed that the distal pocket in Mb allows for different conformations of the NO ligand (120 degrees and 144 degrees ) in Mb(II)NO depending on the mode of preparation of the compound. In this article, we report the crystal structures of the nitrite and NO adducts of manganese-substituted hh Mb (a d(4) system) and of the nitrite adduct of cobalt-substituted hh Mb (a d(6) system). We show that the distal His64 residue directs the nitrite ligand towards the rare nitrito O-binding mode in Mn(III)Mb and Co(III)Mb. We also report that the distal pocket residues allow a stabilization of an unprecendented bent MnNO moiety in Mn(II)MbNO. These crystal structural data, when combined with the data for the aquo, methanol, and azide MnMb derivatives, provide information on the role of distal pocket residues in the observed binding modes of nitrite and NO ligands to wild-type and metal-substituted Mb.

Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations.,Zahran ZN, Chooback L, Copeland DM, West AH, Richter-Addo GB J Inorg Biochem. 2008 Feb;102(2):216-33. Epub 2007 Aug 25. PMID:17905436[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Zahran ZN, Chooback L, Copeland DM, West AH, Richter-Addo GB. Crystal structures of manganese- and cobalt-substituted myoglobin in complex with NO and nitrite reveal unusual ligand conformations. J Inorg Biochem. 2008 Feb;102(2):216-33. Epub 2007 Aug 25. PMID:17905436 doi:10.1016/j.jinorgbio.2007.08.002

2o5o, resolution 1.60Å

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