1mwc: Difference between revisions

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<StructureSection load='1mwc' size='340' side='right'caption='[[1mwc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1mwc' size='340' side='right'caption='[[1mwc]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mwc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWC FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mwc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MWC FirstGlance]. <br>
</td></tr><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></td></tr>
</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>
<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></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=1mwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwc OCA], [https://pdbe.org/1mwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwc RCSB], [https://www.ebi.ac.uk/pdbsum/1mwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwc ProSAT]</span></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=1mwc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwc OCA], [https://pdbe.org/1mwc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mwc RCSB], [https://www.ebi.ac.uk/pdbsum/1mwc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mwc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/MYG_PIG MYG_PIG]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.  
[https://www.uniprot.org/uniprot/MYG_PIG MYG_PIG] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1mwc ConSurf].
</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=1mwc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The isopropyl side chain of valine68 in myoglobin has been replaced by the acetamide side chain of asparagine in an attempt to engineer higher oxygen affinity. The asparagine replacement introduces a second hydrogen bond donor group into the distal heme pocket which could further stabilize bound oxygen. The Val68 to Asn substitution leads to approximately 3-fold increases in oxygen affinity and 4-6-fold decreases in CO affinity. As a result, the M-value (KCO/KO2) is lowered 15-20-fold to a value close to unity. An even larger enhancement of O2 affinity is seen when asparagine68 is inserted into H64L sperm whale myoglobin which lacks a distal histidine. The overall rate constants for oxygen and carbon monoxide binding to the single V68N myoglobin mutants are uniformly lower than those for the wild-type protein. In contrast, the overall rate constant for NO association is unchanged. Analyses of time courses monitoring the geminate recombination of ligands following nanosecond and picosecond flash photolysis of MbNO and MbO2 indicate that the barrier to ligand binding from within the heme pocket has been raised with little effect on the barrier to diffusion of the ligand into the pocket from the solvent. The crystal structures of the aquomet, deoxy, oxy, and carbon monoxy forms of the V68N mutant have been determined to resolutions ranging from 1.75 to 2.2 A at 150 K. The overall structures are very similar to those of the wild-type protein with the principal alterations taking place within and around the distal heme pocket. In all four structures the asparagine68 side chain lies almost parallel to the plane of the heme with its amide group directed toward the back of the distal heme pocket. The coordinated water molecule in the aquomet form and the bound oxygen in the oxy form can form hydrogen-bonding interactions with both the Asn68 amide group and the imidazole side chain of His64. Surprisingly, in the carbon monoxy form of the V68N mutant, the histidine64 side chain has swung completely out the distal pocket, its place being taken by two ordered water molecules. Overall, these functional and structural results show that the asparagine68 side chain (i) forms a strong hydrogen bond with bound oxygen through its -NH2 group but (ii) sterically hinders the approach of ligands to the iron from within the distal heme pocket.
Stabilizing bound O2 in myoglobin by valine68 (E11) to asparagine substitution.,Krzywda S, Murshudov GN, Brzozowski AM, Jaskolski M, Scott EE, Klizas SA, Gibson QH, Olson JS, Wilkinson AJ Biochemistry. 1998 Nov 10;37(45):15896-907. PMID:9843395<ref>PMID:9843395</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mwc" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pig]]
[[Category: Sus scrofa]]
[[Category: Brzozowski, A M]]
[[Category: Brzozowski AM]]
[[Category: Gibson, Q H]]
[[Category: Gibson QH]]
[[Category: Jaskolski, M]]
[[Category: Jaskolski M]]
[[Category: Klizas, S A]]
[[Category: Klizas SA]]
[[Category: Krzywda, S]]
[[Category: Krzywda S]]
[[Category: Murshudov, G N]]
[[Category: Murshudov GN]]
[[Category: Olson, J S]]
[[Category: Olson JS]]
[[Category: Scott, E E]]
[[Category: Scott EE]]
[[Category: Wilkinson, A J]]
[[Category: Wilkinson AJ]]
[[Category: Co]]
[[Category: Myoglobin]]
[[Category: Oxygen storage-transport complex]]

Latest revision as of 10:49, 14 February 2024

WILD TYPE MYOGLOBIN WITH COWILD TYPE MYOGLOBIN WITH CO

Structural highlights

1mwc is a 2 chain structure with sequence from Sus scrofa. 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_PIG 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

1mwc, resolution 1.70Å

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