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[[Image:1mym.gif|left|200px]]


{{Structure
==STRUCTURAL DETERMINANTS OF CO STRETCHING VIBRATION FREQUENCIES IN MYOGLOBIN==
|PDB= 1mym |SIZE=350|CAPTION= <scene name='initialview01'>1mym</scene>, resolution 1.7&Aring;
<StructureSection load='1mym' size='340' side='right'caption='[[1mym]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=CMO:CARBON MONOXIDE'>CMO</scene>
<table><tr><td colspan='2'>[[1mym]] 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=1MYM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MYM 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]] 1.7&#8491;</td></tr>
|GENE= SYNTHETIC GENE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9755 Physeter catodon])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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=1mym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mym OCA], [https://pdbe.org/1mym PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mym RCSB], [https://www.ebi.ac.uk/pdbsum/1mym PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mym 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/my/1mym_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=1mym ConSurf].
<div style="clear:both"></div>


'''STRUCTURAL DETERMINANTS OF CO STRETCHING VIBRATION FREQUENCIES IN MYOGLOBIN'''
==See Also==
 
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
In order to assess the relative importance of polar versus steric interactions, infrared spectra and overall CO binding properties were measured at room temperature for 41 different recombinant myoglobins containing mutations at His64(E7), Val68(E11), Phe43(CD1), Arg45(CD3), Phe46(CD4), and Leu29(B10). The results were compared to the crystal structures of wild-type, Phe29, Val46, Ala68, Phe68, Gln64, Leu64, and Gly64 sperm whale CO-myoglobin and that of Thr68 pig CO-myoglobin. As observed in several previous studies, replacement of the distal histidine (His64) with aliphatic amino acids results in the appearance of a single IR band in the 1960-1970-cm-1 region and in large increases in CO affinity (KCO). More complex behavior is observed for Gly, Ala, Gln, Met, and Trp substitutions at position 64, but in each case there is a net increase in the intensity of this high-frequency component. Replacement of Val68 with Ala, Leu, Ile, and Phe produces little effect on the IR spectrum, whereas these mutations cause 20-fold changes in KCO, presumably due to steric effects. Replacement of Val68 with Thr decreases KCO 4-5-fold, whereas the position of the major IR band increases from 1945 to 1961 cm-1. Replacement of Val68 with Asn also causes a large decrease in KCO, but in this case, the peak position of the major IR band decreases from 1945 to 1916 cm-1. Nine replacements were made in the CD corner at positions 43, 45, and 46. All of the resultant mutants show increased stretching frequencies that can be correlated with movement of the imidazole side chain of His64 away from the bound ligand. All five substitutions at position 29 cause changes in the IR spectra. The Leu29--&gt;Phe mutation had the largest effect, producing a single band centered at 1932 cm-1. Together these data demonstrate that there is little direct correlation between affinity, vCO, and Fe-C-O geometry. The major factor governing vCO appears to be the electrostatic potential surrounding the bound ligand and not steric hindrance. The presence of positive charges from proton donors, such as N epsilon of His64 and N delta of Asn68, cause a decrease in the bond order and stretching frequency of bound CO. In contrast, the negative portion of the Thr68 dipole points directly toward the bound ligand and increases the C-O bond order and stretching frequency. Movement of His64 away from the bound ligand or replacement of this residue with aliphatic amino acids prevents hydrogen-bonding interactions, causing vCO to increase.(ABSTRACT TRUNCATED AT 250 WORDS)
[[Category: Large Structures]]
 
==About this Structure==
1MYM 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=1MYM OCA].
 
==Reference==
Structural determinants of the stretching frequency of CO bound to myoglobin., Li T, Quillin ML, Phillips GN Jr, Olson JS, Biochemistry. 1994 Feb 15;33(6):1433-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8312263 8312263]
[[Category: Physeter catodon]]
[[Category: Physeter catodon]]
[[Category: Single protein]]
[[Category: Li T]]
[[Category: Jr., G N.Phillips.]]
[[Category: Phillips Jr GN]]
[[Category: Li, T.]]
[[Category: CMO]]
[[Category: HEM]]
[[Category: SO4]]
[[Category: oxygen transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:49:51 2008''

Latest revision as of 10:50, 14 February 2024

STRUCTURAL DETERMINANTS OF CO STRETCHING VIBRATION FREQUENCIES IN MYOGLOBINSTRUCTURAL DETERMINANTS OF CO STRETCHING VIBRATION FREQUENCIES IN MYOGLOBIN

Structural highlights

1mym is a 1 chain structure with sequence from Physeter catodon. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYG_PHYMC 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.

See Also

1mym, resolution 1.70Å

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