3nh6: Difference between revisions

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-[[Image:3nh6.png|left|200px]]
-<!--
+==Nucleotide Binding Domain of human ABCB6 (apo structure)==
-The line below this paragraph, containing "STRUCTURE_3nh6", creates the "Structure Box" on the page.
+<StructureSection load='3nh6' size='340' side='right'caption='[[3nh6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3nh6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NH6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NH6 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene></td></tr>
-{{STRUCTURE_3nh6|  PDB=3nh6  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3nh6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nh6 OCA], [https://pdbe.org/3nh6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nh6 RCSB], [https://www.ebi.ac.uk/pdbsum/3nh6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nh6 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/ABCB6_HUMAN ABCB6_HUMAN] Ocular coloboma;Dyschromatosis universalis;Colobomatous microphthalmia. The disease is caused by mutations affecting the gene represented in this entry.  The disease is caused by mutations affecting the gene represented in this entry.  ABCB6 mutations are involved in familial pseudohyperkalemia, a dominantly inherited condition characterized by increased serum potassium levels, measured in whole-blood specimens stored at or below room temperature. This condition is not accompanied by clinical symptoms or biological signs except for borderline abnormalities of red cell shape (PubMed:23180570).<ref>PMID:23180570</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/ABCB6_HUMAN ABCB6_HUMAN] Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis.<ref>PMID:10837493</ref> <ref>PMID:17006453</ref>
+== 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/nh/3nh6_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=3nh6 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The human ATP-binding cassette (ABC) transporter ABCB6 is involved in haem-precursor transport across the mitochondrial membrane. The crystal structure of its nucleotide-binding domain (NBD) has been determined in the apo form and in complexes with ADP, with ADP and Mg(2+) and with ATP at high resolution. The overall structure is L-shaped and consists of two lobes, consistent with other reported NBD structures. Nucleotide binding is mediated by the highly conserved Tyr599 and the Walker A motif, and induces notable structural changes. Structural comparison with other structurally characterized NBDs and full-length ABC transporters gives the first insight into the possible catalytic mechanism of ABCB6 and the role of the N-terminal helix alpha(1) in full-length ABCB6.
-===Nucleotide Binding Domain of human ABCB6 (apo structure)===
+Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides.,Haffke M, Menzel A, Carius Y, Jahn D, Heinz DW Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):979-87. Epub 2010 Aug 13. PMID:20823549<ref>PMID:20823549</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_20823549}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3nh6" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 20823549 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_20823549}}
-==About this Structure==
-[[3nh6]] is a 1 chain structure of [[ABC transporter]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NH6 OCA].
 ==See Also==
-*[[ABC transporter]]
+*[[ABC transporter 3D structures|ABC transporter 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:020823549</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Carius, Y.]]
+[[Category: Large Structures]]
-[[Category: Haffke, M.]]
+[[Category: Carius Y]]
-[[Category: Heinz, D W.]]
+[[Category: Haffke M]]
-[[Category: Jahn, D.]]
+[[Category: Heinz DW]]
-[[Category: Menzel, A.]]
+[[Category: Jahn D]]
-[[Category: Abc-transporter]]
+[[Category: Menzel A]]
-[[Category: Abcb6]]
-[[Category: Heme biosynthesis]]
-[[Category: Nucleotide binding domain]]
-[[Category: Transport protein]]