1dti: Difference between revisions

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-[[Image:1dti.png|left|200px]]
-<!--
+==Recombinant sperm whale myoglobin h97d, d122n mutant (met)==
-The line below this paragraph, containing "STRUCTURE_1dti", creates the "Structure Box" on the page.
+<StructureSection load='1dti' size='340' side='right'caption='[[1dti]], [[Resolution|resolution]] 1.70&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'>[[1dti]] 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=1DTI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DTI 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]] 1.7&#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></td></tr>
-{{STRUCTURE_1dti|  PDB=1dti  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dti FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dti OCA], [https://pdbe.org/1dti PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dti RCSB], [https://www.ebi.ac.uk/pdbsum/1dti PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dti 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/dt/1dti_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=1dti ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The ability of myoglobin to bind oxygen reversibly depends critically on retention of the heme prosthetic group. Globin side chains at the Leu(89)(F4), His(97)(FG3), Ile(99)(FG5), and Leu(104)(G5) positions on the proximal side of the heme pocket strongly influence heme affinity. The roles of these amino acids in preventing heme loss have been examined by determining high resolution structures of 14 different mutants at these positions using x-ray crystallography. Leu(89) and His(97) are important surface amino acids that interact either sterically or electrostatically with the edges of the porphyrin ring. Ile(99) and Leu(104) are located in the interior region of the proximal pocket beneath ring C of the heme prosthetic group. The apolar amino acids Leu(89), Ile(99), and Leu(104) "waterproof" the heme pocket by forming a barrier to solvent penetration, minimizing the size of the proximal cavity, and maintaining a hydrophobic environment. Substitutions with smaller or polar side chains at these positions result in exposure of the heme to solvent, the appearance of crystallographically defined water molecules in or near the proximal pocket, and large increases in the rate of hemin loss. Thus, the naturally occurring amino acid side chains at these positions serve to prevent hydration of the His(93)-Fe(III) bond and are highly conserved in all known myoglobins and hemoglobins.
-===Recombinant sperm whale myoglobin h97d, d122n mutant (met)===
+Waterproofing the heme pocket. Role of proximal amino acid side chains in preventing hemin loss from myoglobin.,Liong EC, Dou Y, Scott EE, Olson JS, Phillips GN Jr J Biol Chem. 2001 Mar 23;276(12):9093-100. Epub 2000 Nov 17. PMID:11084036<ref>PMID:11084036</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_11084036}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1dti" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11084036 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_11084036}}
-==About this Structure==
-[[1dti]] is a 1 chain structure of [[Myoglobin]] with 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=1DTI OCA].
 ==See Also==
-*[[Myoglobin]]
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:11084036</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Physeter catodon]]
-[[Category: Liong, E C.]]
+[[Category: Liong EC]]
-[[Category: Phillips, G N.]]
+[[Category: Phillips Jr GN]]
-[[Category: Heme]]
-[[Category: Muscle protein]]
-[[Category: Oxygen storage/transport complex]]
-[[Category: Oxygen transport]]