2e7d: Difference between revisions

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 <StructureSection load='2e7d' size='340' side='right'caption='[[2e7d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2e7d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E7D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2e7d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E7D FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2h3k|2h3k]], [[2o1a|2o1a]], [[2ite|2ite]], [[2itf|2itf]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IsdH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1280 "Micrococcus aureus" (Rosenbach 1884) Zopf 1885])</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=2e7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e7d OCA], [https://pdbe.org/2e7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e7d RCSB], [https://www.ebi.ac.uk/pdbsum/2e7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e7d ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/ISDH_STAAM ISDH_STAAM]] Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone (By similarity).
+[https://www.uniprot.org/uniprot/ISDH_STAAM ISDH_STAAM] Binds human plasma haptoglobin-hemoglobin complexes, haptoglobin and hemoglobin. Binds haptoglobin-hemoglobin complexes with significantly higher affinity than haptoglobin alone (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=2e7d ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-To elucidate the heme acquisition system in pathogenic bacteria, we investigated the heme-binding properties of the third NEAT domain of IsdH (IsdH-NEAT3), a receptor for heme located on the surfaces of pathogenic bacterial cells, by using x-ray crystallography, isothermal titration calorimetry, examination of absorbance spectra, mutation analysis, size-exclusion chromatography, and analytical ultracentrifugation. We found the following: 1) IsdH-NEAT3 can bind with multiple heme molecules by two modes; 2) heme was bound at the surface of IsdH-NEAT3; 3) candidate residues proposed from the crystal structure were not essential for binding with heme; and 4) IsdH-NEAT3 was associated into a multimeric heme complex by the addition of excess heme. From these observations, we propose a heme-binding mechanism for IsdH-NEAT3 that involves multimerization and discuss the biological importance of this mechanism.
-Structural basis for multimeric heme complexation through a specific protein-heme interaction: the case of the third neat domain of IsdH from Staphylococcus aureus.,Watanabe M, Tanaka Y, Suenaga A, Kuroda M, Yao M, Watanabe N, Arisaka F, Ohta T, Tanaka I, Tsumoto K J Biol Chem. 2008 Oct 17;283(42):28649-59. Epub 2008 Jul 30. PMID:18667422<ref>PMID:18667422</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2e7d" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Kumagai, I]]
+[[Category: Staphylococcus aureus]]
-[[Category: Suenaga, A]]
+[[Category: Kumagai I]]
-[[Category: Tanaka, I]]
+[[Category: Suenaga A]]
-[[Category: Tanaka, Y]]
+[[Category: Tanaka I]]
-[[Category: Tsumoto, K]]
+[[Category: Tanaka Y]]
-[[Category: Yao, M]]
+[[Category: Tsumoto K]]
-[[Category: Ig-like fold]]
+[[Category: Yao M]]
-[[Category: Metal binding protein]]