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New page: left|200px<br /> <applet load="1s6a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s6a, resolution 1.69Å" /> '''The X-ray structure...
 
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[[Image:1s6a.gif|left|200px]]<br />
<applet load="1s6a" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1s6a, resolution 1.69&Aring;" />
'''The X-ray structure of the cyanobacteria Synechocystis hemoglobin "cyanoglobin" with azide ligand'''<br />


==Overview==
==The X-ray structure of the cyanobacteria Synechocystis hemoglobin "cyanoglobin" with azide ligand==
The crystal structures of cyanide and azide-bound forms of the truncated, hemoglobin from Synechocystis are presented at 1.8 angstroms resolution. A, comparison with the structure of the endogenously liganded protein reveals, a conformational shift unprecedented in hemoglobins, and provides the, first picture of a hexacoordinate hemoglobin in both the bis-histidyl and, the exogenously coordinated states. The structural changes between the, different conformations are confined to two regions of the protein; the B, helix, and the E helix, including the EF loop. A molecular "hinge", controlling movement of the E helix is observed in the EF loop, which is, composed of three principal structural elements: Arg64, the, heme-d-propionate, and a three-residue extension of the F helix., Additional features of the structural transition between the two protein, conformations are discussed as they relate to the complex ligand-binding, behavior observed in hexacoordinate hemoglobins, and the potential, physiological function of this class of proteins.
<StructureSection load='1s6a' size='340' side='right'caption='[[1s6a]], [[Resolution|resolution]] 1.69&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1s6a]] 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=1S6A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S6A FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.69&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</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=1s6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6a OCA], [https://pdbe.org/1s6a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s6a RCSB], [https://www.ebi.ac.uk/pdbsum/1s6a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s6a ProSAT]</span></td></tr>
</table>
== Function ==
[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).
== 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/s6/1s6a_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1s6a ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structures of cyanide and azide-bound forms of the truncated hemoglobin from Synechocystis are presented at 1.8 angstroms resolution. A comparison with the structure of the endogenously liganded protein reveals a conformational shift unprecedented in hemoglobins, and provides the first picture of a hexacoordinate hemoglobin in both the bis-histidyl and the exogenously coordinated states. The structural changes between the different conformations are confined to two regions of the protein; the B helix, and the E helix, including the EF loop. A molecular "hinge" controlling movement of the E helix is observed in the EF loop, which is composed of three principal structural elements: Arg64, the heme-d-propionate, and a three-residue extension of the F helix. Additional features of the structural transition between the two protein conformations are discussed as they relate to the complex ligand-binding behavior observed in hexacoordinate hemoglobins, and the potential physiological function of this class of proteins.


==About this Structure==
Crystallographic analysis of synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin.,Trent JT 3rd, Kundu S, Hoy JA, Hargrove MS J Mol Biol. 2004 Aug 20;341(4):1097-108. PMID:15289104<ref>PMID:15289104</ref>
1S6A 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 FLC, AZI 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=1S6A OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystallographic analysis of synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin., Trent JT 3rd, Kundu S, Hoy JA, Hargrove MS, J Mol Biol. 2004 Aug 20;341(4):1097-108. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15289104 15289104]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1s6a" style="background-color:#fffaf0;"></div>
[[Category: Synechocystis sp.]]
[[Category: Hargrove, M.S.]]
[[Category: Hoy, J.A.]]
[[Category: III, J.T.Trent.]]
[[Category: Kundu, S.]]
[[Category: AZI]]
[[Category: FLC]]
[[Category: HEM]]
[[Category: 2 on 2 helical fold]]
[[Category: cyanobacteria]]
[[Category: globin]]
[[Category: heme]]
[[Category: hemoglobin]]
[[Category: hexacoordinate]]
[[Category: iron]]
[[Category: oxygen binding]]
[[Category: truncated]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 13:17:50 2007''
==See Also==
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synechocystis sp. PCC 6803]]
[[Category: Hargrove MS]]
[[Category: Hoy JA]]
[[Category: Kundu S]]
[[Category: Trent III JT]]
Retrieved from "https://proteopedia.org/1s6a"