View source for 3arj


==Cl- binding hemoglobin component V form Propsilocerus akamusi under 500 mM NaCl at pH 4.6==
<StructureSection load='3arj' size='340' side='right'caption='[[3arj]], [[Resolution|resolution]] 1.81&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3arj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tokunagayusurika_akamusi Tokunagayusurika akamusi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ARJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ARJ 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]] 1.81&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=3arj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3arj OCA], [https://pdbe.org/3arj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3arj RCSB], [https://www.ebi.ac.uk/pdbsum/3arj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3arj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q7M422_9DIPT Q7M422_9DIPT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Monomeric haemoglobin component V (Hb V) from the larva of the midge Propsilocerus akamusi shows high Cl affinity under high salt concentrations at acidic pH. In order to understand the structural changes that depend on Cl binding, crystal structures of Hb V were determined under acidic high-salt conditions and the structural changes arising from different haem-bound ligands were simulated. Crystal structures of Hb V under acidic high-salt conditions indicated that the side chain of ArgE10 on the distal face of the haem contributes to stabilizing haem-bound Cl. The conformation of the Arg side chain in the Cl-bound form was almost identical to that in ligated Hb V at neutral pH but not to that in met Hb V under acidic salt-free conditions. Furthermore, preliminary molecular-dynamics simulations also indicated that the swinging of the Arg side chain into the haem pocket depends on Cl ligation. This result suggests that, like pH change, Cl binding affects the location of the distal Arg residue. Owing to the increased positive electrostatic potential observed in the haem pocket at acidic pH, it was concluded that electrostatic changes caused by pH change and anionic ligand binding may affect the behaviour of the polar Arg residue.

Involvement of the distal Arg residue in Cl binding of midge larval haemoglobin.,Kuwada T, Hasegawa T, Takagi T, Sakae T, Sato I, Shishikura F Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):488-95. Epub 2011 Apr 16. PMID:21543852<ref>PMID:21543852</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3arj" style="background-color:#fffaf0;"></div>

==See Also==
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tokunagayusurika akamusi]]
[[Category: Hasegawa T]]
[[Category: Kuwada T]]
[[Category: Shishikura F]]
[[Category: Takagi T]]