1qjs: Difference between revisions

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-[[Image:1qjs.jpg|left|200px]]<br /><applet load="1qjs" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1qjs, resolution 2.9&Aring;" />
-'''MAMMALIAN BLOOD SERUM HAEMOPEXIN GLYCOSYLATED-NATIVE PROTEIN AND IN COMPLEX WITH ITS LIGAND HAEM'''<br />
-==Overview==
+==mammalian blood serum haemopexin glycosylated-native protein and in complex with its ligand haem==
-The ubiquitous use of heme in animals poses severe biological and chemical, challenges. Free heme is toxic to cells and is a potential source of iron, for pathogens. For protection, especially in conditions of trauma, inflammation and hemolysis, and to maintain iron homeostasis, a, high-affinity binding protein, hemopexin, is required. Hemopexin binds, heme with the highest affinity of any known protein, but releases it into, cells via specific receptors. The crystal structure of the heme-hemopexin, complex reveals a novel heme binding site, formed between two similar, four-bladed beta-propeller domains and bounded by the interdomain linker., The ligand is bound to two histidine residues in a pocket dominated by, aromatic and basic groups. Further stabilization is achieved by the, association of the two beta-propeller domains, which form an extensive, polar interface that includes a cushion of ordered water molecules. We, propose mechanisms by which these structural features provide the dual, function of heme binding and release.
+<StructureSection load='1qjs' size='340' side='right'caption='[[1qjs]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1qjs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJS 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]] 2.9&#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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=1qjs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qjs OCA], [https://pdbe.org/1qjs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qjs RCSB], [https://www.ebi.ac.uk/pdbsum/1qjs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qjs ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/HEMO_RABIT HEMO_RABIT] Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.
+== 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/qj/1qjs_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1qjs ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The ubiquitous use of heme in animals poses severe biological and chemical challenges. Free heme is toxic to cells and is a potential source of iron for pathogens. For protection, especially in conditions of trauma, inflammation and hemolysis, and to maintain iron homeostasis, a high-affinity binding protein, hemopexin, is required. Hemopexin binds heme with the highest affinity of any known protein, but releases it into cells via specific receptors. The crystal structure of the heme-hemopexin complex reveals a novel heme binding site, formed between two similar four-bladed beta-propeller domains and bounded by the interdomain linker. The ligand is bound to two histidine residues in a pocket dominated by aromatic and basic groups. Further stabilization is achieved by the association of the two beta-propeller domains, which form an extensive polar interface that includes a cushion of ordered water molecules. We propose mechanisms by which these structural features provide the dual function of heme binding and release.
-==About this Structure==
+Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains.,Paoli M, Anderson BF, Baker HM, Morgan WT, Smith A, Baker EN Nat Struct Biol. 1999 Oct;6(10):926-31. PMID:10504726<ref>PMID:10504726</ref>
-QJS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with PO4, CL, NA and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=HIA:Axial Haem Ligands, Chain A'>HIA</scene> and <scene name='pdbsite=HIB:Axial Haem Ligands, Chain B'>HIB</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QJS OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Crystal structure of hemopexin reveals a novel high-affinity heme site formed between two beta-propeller domains., Paoli M, Anderson BF, Baker HM, Morgan WT, Smith A, Baker EN, Nat Struct Biol. 1999 Oct;6(10):926-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10504726 10504726]
+</div>
+<div class="pdbe-citations 1qjs" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[Category: Oryctolagus cuniculus]]
-[[Category: Single protein]]
+[[Category: Baker EN]]
-[[Category: Baker, E.N.]]
+[[Category: Baker HM]]
-[[Category: Baker, H.M.]]
+[[Category: Morgan WT]]
-[[Category: Morgan, W.T.]]
+[[Category: Paoli M]]
-[[Category: Paoli, M.]]
+[[Category: Smith A]]
-[[Category: Smith, A.]]
-[[Category: CL]]
-[[Category: HEM]]
-[[Category: NA]]
-[[Category: PO4]]
-[[Category: beta propeller]]
-[[Category: haem binding and transport]]
-[[Category: iron metabolism]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:54:36 2007''