| Structural highlights
3nha is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , , , |
| Related: | 3nh6, 3nh9, 3nhb |
| Gene: | ABCB6, MTABC3, PRP, UMAT (HUMAN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Disease
[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).[1]
Function
[ABCB6_HUMAN] Binds heme and porphyrins and functions in their ATP-dependent uptake into the mitochondria. Plays a crucial role in heme synthesis.[2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
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[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Andolfo I, Alper SL, Delaunay J, Auriemma C, Russo R, Asci R, Esposito MR, Sharma AK, Shmukler BE, Brugnara C, De Franceschi L, Iolascon A. Missense mutations in the ABCB6 transporter cause dominant familial pseudohyperkalemia. Am J Hematol. 2013 Jan;88(1):66-72. doi: 10.1002/ajh.23357. Epub 2012 Nov 24. PMID:23180570 doi:http://dx.doi.org/10.1002/ajh.23357
- ↑ Mitsuhashi N, Miki T, Senbongi H, Yokoi N, Yano H, Miyazaki M, Nakajima N, Iwanaga T, Yokoyama Y, Shibata T, Seino S. MTABC3, a novel mitochondrial ATP-binding cassette protein involved in iron homeostasis. J Biol Chem. 2000 Jun 9;275(23):17536-40. PMID:10837493
- ↑ Krishnamurthy PC, Du G, Fukuda Y, Sun D, Sampath J, Mercer KE, Wang J, Sosa-Pineda B, Murti KG, Schuetz JD. Identification of a mammalian mitochondrial porphyrin transporter. Nature. 2006 Oct 5;443(7111):586-9. Epub 2006 Sep 27. PMID:17006453 doi:http://dx.doi.org/10.1038/nature05125
- ↑ Haffke M, Menzel A, Carius Y, Jahn D, Heinz DW. Structures of the nucleotide-binding domain of the human ABCB6 transporter and its complexes with nucleotides. Acta Crystallogr D Biol Crystallogr. 2010 Sep;66(Pt 9):979-87. Epub 2010 Aug 13. PMID:20823549 doi:10.1107/S0907444910028593
|
