1hsy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:30, 7 February 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1hsy.jpg|left|200px]]
 
-
<!--
+
==ORIGIN OF THE PH-DEPENDENT SPECTROSCOPIC PROPERTIES OF PENTACOORDINATE METMYOGLOBIN VARIANTS==
-
The line below this paragraph, containing "STRUCTURE_1hsy", creates the "Structure Box" on the page.
+
<StructureSection load='1hsy' size='340' side='right'caption='[[1hsy]], [[Resolution|resolution]] 1.90&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'>[[1hsy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HSY 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]] 1.9&#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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
{{STRUCTURE_1hsy| PDB=1hsy | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hsy OCA], [https://pdbe.org/1hsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hsy RCSB], [https://www.ebi.ac.uk/pdbsum/1hsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hsy ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/MYG_HORSE MYG_HORSE] 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/hs/1hsy_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=1hsy ConSurf].
 +
<div style="clear:both"></div>
-
'''ORIGIN OF THE PH-DEPENDENT SPECTROSCOPIC PROPERTIES OF PENTACOORDINATE METMYOGLOBIN VARIANTS'''
+
==See Also==
-
 
+
*[[Myoglobin 3D structures|Myoglobin 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
The pH dependence of the electronic and EPR spectra of two variants of horse heart myoglobin (Mb) in which the distal His64 ligand has been replaced by either Thr or Ile has been studied. Both of these variants exhibit spectroscopic changes with pH that are indicative of a transition between two ferric high-spin forms that occurs with a pKa of 9.49 for the His64Thr variant and 9.26 for the His64Ile variant and that is distinctly different from the pH-dependent spectroscopic changes related to titration of the distal aquo ligand of wild-type Mb. The electronic and EPR spectra of both variants at all values of pH studied are consistent with the presence of a pentacoordinate heme iron center. For the His64Thr variant, a high-resolution (1.9 A) structure determination establishes the lack of the distal aquo ligand and demonstrates an out-of-plane movement of the ferric iron toward the proximal histidine together with a decrease of the Fe-His bond length. Investigation of this pH-linked equilibrium by EPR spectroscopy reveals rhombically split high-spin signals at both pH 7 and 11 with a greater degree of rhombicity exhibited by the alkaline species. We propose that the pH-linked spectroscopic transition exhibited by these distal histidine variants results from the deprotonation of the proximal His93 residue to produce imidazolate ligation at alkaline pH.
+
-
 
+
-
==About this Structure==
+
-
1HSY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSY OCA].
+
-
 
+
-
==Reference==
+
-
Origin of the pH-dependent spectroscopic properties of pentacoordinate metmyoglobin variants., Bogumil R, Maurus R, Hildebrand DP, Brayer GD, Mauk AG, Biochemistry. 1995 Aug 22;34(33):10483-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7654702 7654702]
+
[[Category: Equus caballus]]
[[Category: Equus caballus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Brayer, G D.]]
+
[[Category: Brayer GD]]
-
[[Category: Maurus, R.]]
+
[[Category: Maurus R]]
-
[[Category: Oxygen transport]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:12:00 2008''
+

Current revision

ORIGIN OF THE PH-DEPENDENT SPECTROSCOPIC PROPERTIES OF PENTACOORDINATE METMYOGLOBIN VARIANTS

PDB ID 1hsy

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/1hsy"
Personal tools