1g08: Difference between revisions

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-[[Image:1g08.gif|left|200px]]
- {{Structure
+==CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 5.0==
-|PDB= 1g08 |SIZE=350|CAPTION= <scene name='initialview01'>1g08</scene>, resolution 1.9&Aring;
+<StructureSection load='1g08' size='340' side='right'caption='[[1g08]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=CMO:CARBON MONOXIDE'>CMO</scene>
+<table><tr><td colspan='2'>[[1g08]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G08 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G08 FirstGlance]. <br>
-|ACTIVITY=
+</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>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <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=1g08 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g08 OCA], [https://pdbe.org/1g08 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g08 RCSB], [https://www.ebi.ac.uk/pdbsum/1g08 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g08 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HBA_BOVIN HBA_BOVIN] Involved in oxygen transport from the lung to the various peripheral tissues.
+== 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/g0/1g08_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=1g08 ConSurf].
+<div style="clear:both"></div>
-'''CARBONMONOXY LIGANDED BOVINE HEMOGLOBIN PH 5.0'''
+==See Also==
+*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Initial crystallographic studies suggested that fully liganded mammalian hemoglobin can adopt only a single quaternary structure, the quaternary R structure. However, more recent crystallographic studies revealed the existence of a second quaternary structure for liganded hemoglobin, the quaternary R2 structure. Since these quaternary structures can be crystallized, both must be energetically accessible structures that coexist in solution. Unanswered questions include (i) the relative abundance of the R and R2 structures under various solution conditions and (ii) whether other quaternary structures are energetically accessible for the liganded alpha(2)beta(2) hemoglobin tetramer. Although crystallographic methods cannot directly answer the first question, they represent the most direct and most accurate approach to answering the second question. We now have determined and refined three different crystal structures of bovine carbonmonoxyhemoglobin. These structures provide clear evidence that the dimer-dimer interface of liganded hemoglobin has a wide range of energetically accessible structures that are related to each other by a simple sliding motion. The dimer-dimer interface acts as a "molecular slide bearing" that allows the two alpha beta dimers to slide back and forth without greatly altering the number or the nature of the intersubunit contacts. Since the general stereochemical features of this interface are not unusual, it is likely that interface sliding of the kind displayed by fully liganded hemoglobin plays important structural and functional roles in many other protein assemblies.
-==About this Structure==
-G08 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G08 OCA].
-==Reference==
-Interface sliding as illustrated by the multiple quaternary structures of liganded hemoglobin., Mueser TC, Rogers PH, Arnone A, Biochemistry. 2000 Dec 19;39(50):15353-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11112521 11112521]
 [[Category: Bos taurus]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Arnone, A.]]
+[[Category: Arnone A]]
-[[Category: Mueser, T C.]]
+[[Category: Mueser TC]]
-[[Category: Rogers, P H.]]
+[[Category: Rogers PH]]
-[[Category: CMO]]
-[[Category: HEM]]
-[[Category: bovine]]
-[[Category: carbonmonoxy]]
-[[Category: hemoglobin]]
-[[Category: liganded]]
-[[Category: protoporphyrin ix]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:20 2008''