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New page: left|200px<br /> <applet load="3sdh" size="450" color="white" frame="true" align="right" spinBox="true" caption="3sdh, resolution 1.4Å" /> '''HIGH RESOLUTION CRYS...
 
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[[Image:3sdh.gif|left|200px]]<br />
<applet load="3sdh" size="450" color="white" frame="true" align="right" spinBox="true"
caption="3sdh, resolution 1.4&Aring;" />
'''HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF A COOPERATIVE DIMERIC HEMOGLOBIN'''<br />


==Overview==
==HIGH RESOLUTION CRYSTALLOGRAPHIC ANALYSIS OF A COOPERATIVE DIMERIC HEMOGLOBIN==
High-resolution crystal structures of the co-operative dimeric hemoglobin, from the blood clam Scapharca inaequivalvis have been determined in the, unliganded (deoxy) and carbon monoxide (CO) liganded states. The deoxy, structure has been refined at 1.6 A resolution to an R-factor of 0.158 and, the CO structure has been refined at 1.4 A resolution to an R-factor of, 0.159. These structures reveal details of the structural transitions, involved in co-operative ligand binding that involve only a minor rotation, of subunits but very striking tertiary changes at the interface. A small, number of residues in the F-helix appear to mediate co-operativity in this, simple hemoglobin. The oxygen affinity of each subunit appears to be, largely dictated by the disposition of phenylalanine 97, whose side-chain, packs in the heme pocket in the deoxy state but is extruded towards the, interface in the CO-liganded structure. Direct involvement of the, ligand-binding heme group is a novel feature of the subunit interface and, appears important for intersubunit communication. Ligation alters the, conformation of the heme propionate groups along with two interacting, residues from the symmetry-related subunit. These two residues, lysine 96, and asparagine 100, link the heme of one subunit with the F-helix of the, second subunit in such a way as to influence the ligand affinity of that, subunit. The interface is highly hydrated by well-ordered water molecules, that are likely to be important in the stabilization of the two, structures.
<StructureSection load='3sdh' size='340' side='right'caption='[[3sdh]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sdh]] is a 2 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=3SDH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SDH 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]] 1.4&#8491;</td></tr>
<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=3sdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sdh OCA], [https://pdbe.org/3sdh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sdh RCSB], [https://www.ebi.ac.uk/pdbsum/3sdh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sdh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLB1_ANAIN GLB1_ANAIN]
== 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/sd/3sdh_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=3sdh ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
High-resolution crystal structures of the co-operative dimeric hemoglobin from the blood clam Scapharca inaequivalvis have been determined in the unliganded (deoxy) and carbon monoxide (CO) liganded states. The deoxy structure has been refined at 1.6 A resolution to an R-factor of 0.158 and the CO structure has been refined at 1.4 A resolution to an R-factor of 0.159. These structures reveal details of the structural transitions involved in co-operative ligand binding that involve only a minor rotation of subunits but very striking tertiary changes at the interface. A small number of residues in the F-helix appear to mediate co-operativity in this simple hemoglobin. The oxygen affinity of each subunit appears to be largely dictated by the disposition of phenylalanine 97, whose side-chain packs in the heme pocket in the deoxy state but is extruded towards the interface in the CO-liganded structure. Direct involvement of the ligand-binding heme group is a novel feature of the subunit interface and appears important for intersubunit communication. Ligation alters the conformation of the heme propionate groups along with two interacting residues from the symmetry-related subunit. These two residues, lysine 96 and asparagine 100, link the heme of one subunit with the F-helix of the second subunit in such a way as to influence the ligand affinity of that subunit. The interface is highly hydrated by well-ordered water molecules that are likely to be important in the stabilization of the two structures.


==About this Structure==
High-resolution crystallographic analysis of a co-operative dimeric hemoglobin.,Royer WE Jr J Mol Biol. 1994 Jan 14;235(2):657-81. PMID:8289287<ref>PMID:8289287</ref>
3SDH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Scapharca_inaequivalvis Scapharca inaequivalvis] with HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1SDH. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3SDH OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
High-resolution crystallographic analysis of a co-operative dimeric hemoglobin., Royer WE Jr, J Mol Biol. 1994 Jan 14;235(2):657-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8289287 8289287]
</div>
[[Category: Scapharca inaequivalvis]]
<div class="pdbe-citations 3sdh" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Royerjunior, W.E.]]
[[Category: CMO]]
[[Category: HEM]]
[[Category: oxygen transport]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 13:34:26 2007''
==See Also==
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Anadara inaequivalvis]]
[[Category: Large Structures]]
[[Category: Royerjunior WE]]
Retrieved from "https://proteopedia.org/3sdh"