3s48: Difference between revisions
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< | ==Human Alpha-Haemoglobin Complexed with the First NEAT Domain of IsdH from Staphylococcus aureus== | ||
<StructureSection load='3s48' size='340' side='right'caption='[[3s48]], [[Resolution|resolution]] 3.05Å' scene=''> | |||
== Structural highlights == | |||
or the | <table><tr><td colspan='2'>[[3s48]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Staphylococcus_aureus_subsp._aureus_MSSA476 Staphylococcus aureus subsp. aureus MSSA476]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S48 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]] 3.05Å</td></tr> | |||
- | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=3s48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s48 OCA], [https://pdbe.org/3s48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s48 RCSB], [https://www.ebi.ac.uk/pdbsum/3s48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s48 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ISDH_STAAS ISDH_STAAS] Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone (Probable). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Adult haemoglobin (Hb) is made up of two alpha and two beta subunits. Mutations that reduce expression of the alpha- or beta-globin genes lead to the conditions alpha- or beta-thalassaemia, respectively. Whilst both conditions are characterized by anaemia of variable severity, other details of their pathophysiology are different, in part owing to the greater stability of the beta chains that is conferred through beta self-association. In contrast, alpha subunits interact weakly, and in the absence of stabilizing quaternary interactions the alpha chain (alpha) is prone to haem loss and denaturation. The molecular contacts that confer weak self-association of alpha have not been determined previously. Here, the first structure of an alpha2 homodimer is reported in complex with one domain of the Hb receptor from Staphylococcus aureus. The alpha2 dimer interface has a highly unusual, approximately linear, arrangement of four His side chains within hydrogen-bonding distance of each other. Some interactions present in the alpha1beta1 dimer interface of native Hb are preserved in the alpha2 dimer. However, a marked asymmetry is observed in the alpha2 interface, suggesting that steric factors limit the number of stabilizing interactions that can form simultaneously across the interface. | |||
The structure of alpha-haemoglobin in complex with a haemoglobin-binding domain from Staphylococcus aureus reveals the elusive alpha-haemoglobin dimerization interface.,Krishna Kumar K, Jacques DA, Guss JM, Gell DA Acta Crystallogr F Struct Biol Commun. 2014 Aug 1;70(Pt 8):1032-7. doi:, 10.1107/S2053230X14012175. Epub 2014 Jul 23. PMID:25084376<ref>PMID:25084376</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3s48" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Haptoglobin receptor|Haptoglobin receptor]] | ||
*[[Hemoglobin 3D structures|Hemoglobin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Staphylococcus aureus]] | [[Category: Large Structures]] | ||
[[Category: Caradoc-Davies | [[Category: Staphylococcus aureus subsp. aureus MSSA476]] | ||
[[Category: Gell | [[Category: Caradoc-Davies TT]] | ||
[[Category: Guss | [[Category: Gell DA]] | ||
[[Category: Jacques | [[Category: Guss JM]] | ||
[[Category: Kumar | [[Category: Jacques DA]] | ||
[[Category: Kumar KK]] | |||
Latest revision as of 20:22, 1 November 2023
Human Alpha-Haemoglobin Complexed with the First NEAT Domain of IsdH from Staphylococcus aureusHuman Alpha-Haemoglobin Complexed with the First NEAT Domain of IsdH from Staphylococcus aureus
Structural highlights
FunctionISDH_STAAS Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone (Probable). Publication Abstract from PubMedAdult haemoglobin (Hb) is made up of two alpha and two beta subunits. Mutations that reduce expression of the alpha- or beta-globin genes lead to the conditions alpha- or beta-thalassaemia, respectively. Whilst both conditions are characterized by anaemia of variable severity, other details of their pathophysiology are different, in part owing to the greater stability of the beta chains that is conferred through beta self-association. In contrast, alpha subunits interact weakly, and in the absence of stabilizing quaternary interactions the alpha chain (alpha) is prone to haem loss and denaturation. The molecular contacts that confer weak self-association of alpha have not been determined previously. Here, the first structure of an alpha2 homodimer is reported in complex with one domain of the Hb receptor from Staphylococcus aureus. The alpha2 dimer interface has a highly unusual, approximately linear, arrangement of four His side chains within hydrogen-bonding distance of each other. Some interactions present in the alpha1beta1 dimer interface of native Hb are preserved in the alpha2 dimer. However, a marked asymmetry is observed in the alpha2 interface, suggesting that steric factors limit the number of stabilizing interactions that can form simultaneously across the interface. The structure of alpha-haemoglobin in complex with a haemoglobin-binding domain from Staphylococcus aureus reveals the elusive alpha-haemoglobin dimerization interface.,Krishna Kumar K, Jacques DA, Guss JM, Gell DA Acta Crystallogr F Struct Biol Commun. 2014 Aug 1;70(Pt 8):1032-7. doi:, 10.1107/S2053230X14012175. Epub 2014 Jul 23. PMID:25084376[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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