1jwn

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[[Image:1jwn.gif|left|200px]]
 
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==Crystal Structure of Scapharca inaequivalvis HbI, I114F Mutant Ligated to Carbon Monoxide.==
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The line below this paragraph, containing "STRUCTURE_1jwn", creates the "Structure Box" on the page.
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<StructureSection load='1jwn' size='340' side='right'caption='[[1jwn]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1jwn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anadara_inaequivalvis Anadara inaequivalvis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWN FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<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>
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{{STRUCTURE_1jwn| PDB=1jwn | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwn OCA], [https://pdbe.org/1jwn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwn RCSB], [https://www.ebi.ac.uk/pdbsum/1jwn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLB1_ANAIN GLB1_ANAIN]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jw/1jwn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1jwn ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of Scapharca inaequivalvis HbI, I114F Mutant Ligated to Carbon Monoxide.'''
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==See Also==
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*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Cooperative ligand binding in the dimeric hemoglobin from the blood clam Scapharca inaequivalvis results primarily from tertiary, rather than quaternary, structural changes. Ligand binding is coupled with conformational changes of key residues, including Phe 97, which is extruded from the proximal heme pocket, and the heme group, which moves deeper into the heme pocket. We have tested the role of the heme movement in cooperative function by mutating Ile 114, at the base of the heme pocket. Replacement of this residue with a Met did not disturb the hemoglobin structure or significantly alter equilibrium ligand binding properties. In contrast, substitution with a Phe at position 114 inhibits the ligand-linked movement of the heme group, and substantially reduces oxygen affinity and cooperativity. As the extent of heme movement to the normal position of the ligated state is diminished, Phe 97 is inhibited from its movement into the interface upon ligand binding. These results indicate a tight coupling between these two key cooperative transitions and suggest that the heme movement may be an obligatory trigger for expulsion of Phe 97 from the heme pocket.
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[[Category: Anadara inaequivalvis]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Cushing L]]
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1JWN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Scapharca_inaequivalvis Scapharca inaequivalvis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWN OCA].
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[[Category: Gibson QH]]
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[[Category: Knapp JE]]
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==Reference==
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[[Category: Royer Jr WE]]
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Restricting the ligand-linked heme movement in Scapharca dimeric hemoglobin reveals tight coupling between distal and proximal contributions to cooperativity., Knapp JE, Gibson QH, Cushing L, Royer WE Jr, Biochemistry. 2001 Dec 11;40(49):14795-805. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11732898 11732898]
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[[Category: Scapharca inaequivalvis]]
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[[Category: Single protein]]
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[[Category: Cushing, L.]]
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[[Category: Gibson, Q H.]]
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[[Category: Jr., W E.Royer.]]
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[[Category: Knapp, J E.]]
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[[Category: Allostery]]
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[[Category: Cooperativity]]
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[[Category: Heme protein]]
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[[Category: Invertebrate hemoglobin]]
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[[Category: Oxygen-binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:00:57 2008''
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Current revision

Crystal Structure of Scapharca inaequivalvis HbI, I114F Mutant Ligated to Carbon Monoxide.

PDB ID 1jwn

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