1ch2

From Proteopedia

(Difference between revisions)

Current revision

RECOMBINANT SPERM WHALE MYOGLOBIN L89F MUTANT (MET)

Structural highlights

1ch2 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 1.8Å
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.

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.

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^[1]

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

References

↑ Liong EC, Dou Y, Scott EE, Olson JS, Phillips GN Jr. Waterproofing the heme pocket. Role of proximal amino acid side chains in preventing hemin loss from myoglobin. J Biol Chem. 2001 Mar 23;276(12):9093-100. Epub 2000 Nov 17. PMID:11084036 doi:http://dx.doi.org/10.1074/jbc.M008593200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ch2"

Categories: Large Structures | Physeter catodon | Liong EC | Phillips Jr GN

@@ Line 1: / Line 1: @@
 ==RECOMBINANT SPERM WHALE MYOGLOBIN L89F MUTANT (MET)==
-<StructureSection load='1ch2' size='340' side='right' caption='[[1ch2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+<StructureSection load='1ch2' size='340' side='right'caption='[[1ch2]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ch2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Phycd Phycd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CH2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CH2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ch2]] 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=1CH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CH2 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.8&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ch2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ch2 OCA], [http://pdbe.org/1ch2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ch2 RCSB], [http://www.ebi.ac.uk/pdbsum/1ch2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ch2 ProSAT]</span></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>, <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=1ch2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ch2 OCA], [https://pdbe.org/1ch2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ch2 RCSB], [https://www.ebi.ac.uk/pdbsum/1ch2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ch2 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYG_PHYMC MYG_PHYMC]] Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
+[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/ch/1ch2_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/1ch2_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 1ch2" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Phycd]]
+[[Category: Large Structures]]
-[[Category: Liong, E C]]
+[[Category: Physeter catodon]]
-[[Category: Phillips, G N]]
+[[Category: Liong EC]]
-[[Category: Heme]]
+[[Category: Phillips Jr GN]]
-[[Category: Muscle protein]]
-[[Category: Oxygen storage-transport complex]]
-[[Category: Oxygen transport]]

1ch2

From Proteopedia

Current revision

RECOMBINANT SPERM WHALE MYOGLOBIN L89F MUTANT (MET)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox