2blh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:17, 9 May 2024) (edit) (undo)
 
(22 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2blh.gif|left|200px]]<br />
 
-
<applet load="2blh" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2blh, resolution 1.77&Aring;" />
 
-
'''LIGAND MIGRATION AND PROTEIN FLUCTUATIONS IN MYOGLOBIN MUTANT L29W'''<br />
 
-
==Overview==
+
==Ligand Migration and Protein Fluctuations in Myoglobin Mutant L29W==
-
We have determined eight X-ray structures of myoglobin mutant L29W at, various experimental conditions. In addition, infrared spectroscopic, experiments are presented, which are discussed in the light of the X-ray, structures. Two distinct conformations of the CO-ligated protein were, identified, giving rise to two stretching bands of heme-bound CO. If L29W, MbCO crystals are illuminated around 180 K, a deoxy species is formed. The, CO molecules migrate to the proximal side of the heme and remain trapped, in the so-called Xe1 cavity upon temperature decrease to 105 K. The, structure of this photoproduct is almost identical to the equilibrium, high-temperature deoxy Mb structure. If the temperature is cycled to, increasingly higher values, CO recombination is observed. Three, intermediate structures have been determined during the rebinding process., Efficient recombination occurs only above 180 K, the characteristic, temperature for the onset of protein dynamics. Rebinding is remarkably, slow because bulky residues His64 and Trp29 block important migration, pathways of the CO molecule.
+
<StructureSection load='2blh' size='340' side='right'caption='[[2blh]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2blh]] 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=2BLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BLH FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#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>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2blh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2blh OCA], [https://pdbe.org/2blh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2blh RCSB], [https://www.ebi.ac.uk/pdbsum/2blh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2blh 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/bl/2blh_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=2blh ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
We have determined eight X-ray structures of myoglobin mutant L29W at various experimental conditions. In addition, infrared spectroscopic experiments are presented, which are discussed in the light of the X-ray structures. Two distinct conformations of the CO-ligated protein were identified, giving rise to two stretching bands of heme-bound CO. If L29W MbCO crystals are illuminated around 180 K, a deoxy species is formed. The CO molecules migrate to the proximal side of the heme and remain trapped in the so-called Xe1 cavity upon temperature decrease to 105 K. The structure of this photoproduct is almost identical to the equilibrium high-temperature deoxy Mb structure. If the temperature is cycled to increasingly higher values, CO recombination is observed. Three intermediate structures have been determined during the rebinding process. Efficient recombination occurs only above 180 K, the characteristic temperature for the onset of protein dynamics. Rebinding is remarkably slow because bulky residues His64 and Trp29 block important migration pathways of the CO molecule.
-
==About this Structure==
+
Ligand migration and protein fluctuations in myoglobin mutant L29W.,Nienhaus K, Ostermann A, Nienhaus GU, Parak FG, Schmidt M Biochemistry. 2005 Apr 5;44(13):5095-105. PMID:15794647<ref>PMID:15794647</ref>
-
2BLH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Physeter_catodon Physeter catodon] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BLH OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Ligand migration and protein fluctuations in myoglobin mutant L29W., Nienhaus K, Ostermann A, Nienhaus GU, Parak FG, Schmidt M, Biochemistry. 2005 Apr 5;44(13):5095-105. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15794647 15794647]
+
</div>
-
[[Category: Physeter catodon]]
+
<div class="pdbe-citations 2blh" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
-
[[Category: Nienhaus, G.U.]]
+
-
[[Category: Nienhaus, K.]]
+
-
[[Category: Ostermann, A.]]
+
-
[[Category: Parak, F.G.]]
+
-
[[Category: Schmidt, M.]]
+
-
[[Category: HEM]]
+
-
[[Category: heme]]
+
-
[[Category: mutant]]
+
-
[[Category: myoglobin]]
+
-
[[Category: oxygen transport]]
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:02:02 2007''
+
==See Also==
 +
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Physeter catodon]]
 +
[[Category: Nienhaus GU]]
 +
[[Category: Nienhaus K]]
 +
[[Category: Ostermann A]]
 +
[[Category: Parak FG]]
 +
[[Category: Schmidt M]]

Current revision

Ligand Migration and Protein Fluctuations in Myoglobin Mutant L29W

PDB ID 2blh

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2blh"
Personal tools