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[[Image:1dm1.jpg|left|200px]]


{{Structure
==2.0 A CRYSTAL STRUCTURE OF THE DOUBLE MUTANT H(E7)V, T(E10)R OF MYOGLOBIN FROM APLYSIA LIMACINA==
|PDB= 1dm1 |SIZE=350|CAPTION= <scene name='initialview01'>1dm1</scene>, resolution 1.99&Aring;
<StructureSection load='1dm1' size='340' side='right'caption='[[1dm1]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene>
<table><tr><td colspan='2'>[[1dm1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aplysia_limacina Aplysia limacina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DM1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DM1 FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.99&#8491;</td></tr>
|GENE=  
<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></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=1dm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dm1 OCA], [https://pdbe.org/1dm1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dm1 RCSB], [https://www.ebi.ac.uk/pdbsum/1dm1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dm1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLB_APLLI GLB_APLLI]
== 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/dm/1dm1_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=1dm1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aplysia limacina myoglobin lacks the distal histidine (His (E7)) and displays a ligand stabilization mechanism based on Arg(E10). The double mutant Val(E7)His-Arg(E10)Thr has been prepared to engineer the role of His(E7), typical of mammalian myoglobins, in a different globin framework. The 2.0 A crystal structure of Val(E7)His-Arg(E10)Thr met-Mb mutant reveals that the His(E7) side chain points out of the distal pocket, providing an explanation for the observed failure to stabilize the Fe(II) bound oxygen in the ferrous myoglobin. Moreover, spectroscopic analysis together with kinetic data on azide binding to met-myoglobin are reported and discussed in terms of the presence of a water molecule at coordination distance from the heme iron.


'''2.0 A CRYSTAL STRUCTURE OF THE DOUBLE MUTANT H(E7)V, T(E10)R OF MYOGLOBIN FROM APLYSIA LIMACINA'''
Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin.,Federici L, Savino C, Musto R, Travaglini-Allocatelli C, Cutruzzola F, Brunori M Biochem Biophys Res Commun. 2000 Mar 5;269(1):58-63. PMID:10694477<ref>PMID:10694477</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dm1" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
Aplysia limacina myoglobin lacks the distal histidine (His (E7)) and displays a ligand stabilization mechanism based on Arg(E10). The double mutant Val(E7)His-Arg(E10)Thr has been prepared to engineer the role of His(E7), typical of mammalian myoglobins, in a different globin framework. The 2.0 A crystal structure of Val(E7)His-Arg(E10)Thr met-Mb mutant reveals that the His(E7) side chain points out of the distal pocket, providing an explanation for the observed failure to stabilize the Fe(II) bound oxygen in the ferrous myoglobin. Moreover, spectroscopic analysis together with kinetic data on azide binding to met-myoglobin are reported and discussed in terms of the presence of a water molecule at coordination distance from the heme iron.
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1DM1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_limacina Aplysia limacina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DM1 OCA].
__TOC__
 
</StructureSection>
==Reference==
Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin., Federici L, Savino C, Musto R, Travaglini-Allocatelli C, Cutruzzola F, Brunori M, Biochem Biophys Res Commun. 2000 Mar 5;269(1):58-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10694477 10694477]
[[Category: Aplysia limacina]]
[[Category: Aplysia limacina]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Brunori, M.]]
[[Category: Brunori M]]
[[Category: Cutruzzola, F.]]
[[Category: Cutruzzola F]]
[[Category: Federici, L.]]
[[Category: Federici L]]
[[Category: Musto, R.]]
[[Category: Musto R]]
[[Category: Savino, C.]]
[[Category: Savino C]]
[[Category: Travaglini-Allocatelli, C.]]
[[Category: Travaglini-Allocatelli C]]
[[Category: HEM]]
[[Category: globin fold]]
 
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Retrieved from "https://proteopedia.org/1dm1"