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2hz3

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(New page: 200px<br /> <applet load="2hz3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hz3, resolution 1.90&Aring;" /> '''The x-ray crystal s...)
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[[Image:2hz3.gif|left|200px]]<br />
 
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<applet load="2hz3" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2hz3, resolution 1.90&Aring;" />
 
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'''The x-ray crystal structure of ferrous Synechocystis hemoglobin H117A mutant with a covalent linkage'''<br />
 
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==Overview==
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==The x-ray crystal structure of ferrous Synechocystis hemoglobin H117A mutant with a covalent linkage==
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Synechocystis hemoglobin contains an unprecedented covalent bond between a, nonaxial histidine side chain (H117) and the heme 2-vinyl. This bond has, been previously shown to stabilize the ferric protein against, denaturation, and also to affect the kinetics of cyanide association., However, it is unclear why Synechocystis hemoglobin would require the, additional degree of stabilization accompanying the His117-heme 2-vinyl, bond because it also displays endogenous bis-histidyl axial heme, coordination, which should greatly assist heme retention. Furthermore, the, mechanism by which the His117-heme 2-vinyl bond affects ligand binding has, not been reported, nor has any investigation of the role of this bond on, the structure and function of the protein in the ferrous oxidation state., Here we report an investigation of the role of the Synechocystis, hemoglobin His117-heme 2-vinyl bond on structure, heme coordination, exogenous ligand binding, and stability in both the ferrous and ferric, oxidation states. Our results reveal that hexacoordinate Synechocystis, hemoglobin lacking this bond is less stable in the ferrous oxidation state, than the ferric, which is surprising in light of our understanding of, pentacoordinate Hb stability, in which the ferric protein is always less, stable. It is also demonstrated that removal of the His117-heme 2-vinyl, bond increases the affinity constant for intramolecular histidine, coordination in the ferric oxidation state, thus presenting greater, competition for the ligand binding site and lowering the observed rate and, affinity constants for exogenous ligands.
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<StructureSection load='2hz3' size='340' side='right'caption='[[2hz3]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2hz3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HZ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HZ3 FirstGlance]. <br>
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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]] 1.9&#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=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO2:SULFUR+DIOXIDE'>SO2</scene></td></tr>
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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=2hz3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hz3 OCA], [https://pdbe.org/2hz3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hz3 RCSB], [https://www.ebi.ac.uk/pdbsum/2hz3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hz3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TRHBN_SYNY3 TRHBN_SYNY3] Forms a very stable complex with oxygen. The oxygen dissociation rate is 0.011 s(-1).
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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/hz/2hz3_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=2hz3 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2HZ3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with CD, SO2 and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HZ3 OCA].
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*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation., Hoy JA, Smagghe BJ, Halder P, Hargrove MS, Protein Sci. 2007 Feb;16(2):250-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17242429 17242429]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Synechocystis sp. PCC 6803]]
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[[Category: Synechocystis sp.]]
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[[Category: Hoy JA]]
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[[Category: Hoy, J.A.]]
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[[Category: CD]]
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[[Category: HEM]]
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[[Category: SO2]]
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[[Category: covalent heme vinyl link]]
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[[Category: ferrous]]
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[[Category: globin]]
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[[Category: heme]]
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[[Category: hemoglobin]]
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[[Category: hexacoordinate]]
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[[Category: synechocystis]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:32:33 2007''
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Current revision

The x-ray crystal structure of ferrous Synechocystis hemoglobin H117A mutant with a covalent linkage

PDB ID 2hz3

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