View source for 3nhb


==Nucleotide Binding Domain of Human ABCB6 (ADP bound structure)==
<StructureSection load='3nhb' size='340' side='right' caption='[[3nhb]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3nhb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NHB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NHB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nh6|3nh6]], [[3nh9|3nh9]], [[3nha|3nha]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABCB6, MTABC3, PRP, UMAT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nhb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nhb OCA], [http://pdbe.org/3nhb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3nhb RCSB], [http://www.ebi.ac.uk/pdbsum/3nhb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3nhb ProSAT]</span></td></tr>
</table>
== Disease ==
[[http://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 ==
[[http://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/3nhb_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=3nhb 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.

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>
<div class="pdbe-citations 3nhb" style="background-color:#fffaf0;"></div>

==See Also==
*[[ABC transporter|ABC transporter]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Carius, Y]]
[[Category: Haffke, M]]
[[Category: Heinz, D W]]
[[Category: Jahn, D]]
[[Category: Menzel, A]]
[[Category: Abc-transporter]]
[[Category: Abcb6]]
[[Category: Heme biosynthesis]]
[[Category: Nucleotide binding domain]]
[[Category: Transport protein]]