3hen: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3hen.jpg|left|200px]]
-<!--
+==Ferric Horse Heart Myoglobin; H64V/V67R Mutant==
-The line below this paragraph, containing "STRUCTURE_3hen", creates the "Structure Box" on the page.
+<StructureSection load='3hen' size='340' side='right'caption='[[3hen]], [[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'>[[3hen]] 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=3HEN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HEN 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=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-{{STRUCTURE_3hen|  PDB=3hen  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hen FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hen OCA], [https://pdbe.org/3hen PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hen RCSB], [https://www.ebi.ac.uk/pdbsum/3hen PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hen 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/he/3hen_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=3hen ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+It is now well-established that mammalian heme proteins are reactive with various nitrogen oxide species and that these reactions may play significant roles in mammalian physiology. For example, the ferrous heme protein myoglobin (Mb) has been shown to reduce nitrite (NO(2)(-)) to nitric oxide (NO) under hypoxic conditions. We demonstrate here that the distal pocket histidine residue (His64) of horse heart metMb(III) (i.e., ferric Mb(III)) has marked effects on the mode of nitrite ion coordination to the iron center. X-ray crystal structures were determined for the mutant proteins metMb(III) H64V (2.0 A resolution) and its nitrite ion adduct metMb(III) H64V-nitrite (1.95 A resolution), and metMb(III) H64V/V67R (1.9 A resolution) and its nitrite ion adduct metMb(III) H64V/V67R-nitrite (2.0 A resolution). These are compared to the known structures of wild-type (wt) hh metMb(III) and its nitrite ion adduct hh metMb(III)-nitrite, which binds NO(2)(-) via an O-atom in a trans-FeONO configuration. Unlike wt metMb(III), no axial H(2)O is evident in either of the metMb(III) mutant structures. In the ferric H64V-nitrite structure, replacement of the distal His residue with Val alters the binding mode of nitrite from the nitrito (O-binding) form in the wild-type protein to a weakly bound nitro (N-binding) form. Reintroducing a H-bonding residue in the H64V/V67R double mutant restores the O-binding mode of nitrite. We have also examined the effects of these mutations on reactivities of the metMb(III)s with cysteine as a reducing agent and of the (ferrous) Mb(II)s with nitrite ion under anaerobic conditions. The Mb(II)s were generated by reduction of the Mb(III) precursors in a second-order reaction with cysteine, the rate constants for this step following the order H64V/V67R &gt; H64V &gt;&gt; wt. The rate constants for the oxidation of the Mb(II)s by nitrite (giving NO as the other product) follow the order wt &gt; H64V/V67R &gt;&gt; H64V and suggest a significant role of the distal pocket H-bonding residue in nitrite reduction.
-===Ferric Horse Heart Myoglobin; H64V/V67R Mutant===
+The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron.,Yi J, Heinecke J, Tan H, Ford PC, Richter-Addo GB J Am Chem Soc. 2009 Dec 23;131(50):18119-28. PMID:19924902<ref>PMID:19924902</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3hen" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_19924902}}, adds the Publication Abstract to the page
+*[[Myoglobin 3D structures|Myoglobin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 19924902 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_19924902}}
+__TOC__
+</StructureSection>
-==About this Structure==
-HEN is a 1 chain 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=3HEN OCA].
-==Reference==
-<ref group="xtra">PMID:19924902</ref><references group="xtra"/>
 [[Category: Equus caballus]]
-[[Category: Richter-Addo, G B.]]
+[[Category: Large Structures]]
-[[Category: Thomas, L M.]]
+[[Category: Richter-Addo GB]]
-[[Category: Yi, J.]]
+[[Category: Thomas LM]]
-[[Category: Ferric myoglobin]]
+[[Category: Yi J]]
-[[Category: H64v/v67r mutant]]
-[[Category: Heme]]
-[[Category: Horse heart]]
-[[Category: Iron]]
-[[Category: Metal-binding]]
-[[Category: Muscle protein]]
-[[Category: Oxygen transport]]
-[[Category: Transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 30 14:25:20 2009''