1PQ4
Crystal structure of ZnuA
1PQ4 の概要
| エントリーDOI | 10.2210/pdb1pq4/pdb |
| 分子名称 | periplasmic binding protein component of an ABC type zinc uptake transporter, ZINC ION (3 entities in total) |
| 機能のキーワード | znua, loop, metal-binding, metal binding protein |
| 由来する生物種 | Synechocystis sp. |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 64422.49 |
| 構造登録者 | Banerjee, S.,Wei, B.,Bhattacharyya-Pakrasi, M.,Pakrasi, H.B.,Smith, T.J. (登録日: 2003-06-17, 公開日: 2003-11-04, 最終更新日: 2024-02-14) |
| 主引用文献 | Banerjee, S.,Wei, B.,Bhattacharyya-Pakrasi, M.,Pakrasi, H.B.,Smith, T.J. Structural Determinants of Metal Specificity in the Zinc Transport Protein ZnuA from Synechocystis 6803. J.Mol.Biol., 333:1061-1069, 2003 Cited by PubMed Abstract: A number of bacterial metal transporters belong to the cluster 9 family of ABC transporters. The residues in the periplasmic domain thought to be involved in metal binding seem highly conserved and yet the transporters have varying metal specificity. To solve this seeming paradox and ascertain how metal specificity is exacted, the structure of ZnuA, the periplasmic domain of a zinc transporter from Synechocystis 6803, has been determined to a resolution of 1.9A. In previously determined structures of homologous proteins, four residues chelate the bound metal. From sequence alignments of the cluster 9 metal transporters, the fourth residue in this metal-binding site, an aspartate, is also present in the appropriate position in the ZnuA sequence. However, this result is misleading, since our structural data indicate that zinc binds via only three histidine residues and the aspartate is replaced by a large hydrophobic cavity. We propose that ZnuA binds zinc over manganese by providing only three ligating residues. ZnuA has a highly charged and mobile loop that protrudes from the protein in the vicinity of the metal-binding site. Similar loops are found in other types of zinc transporters but not manganese transporters. Therefore, we propose that the function of this domain is to act as a zinc chaperone to facilitate acquisition. Therefore, while Mn2+ transporters can bind Zn2+ in vitro they may not be able to acquire it in vivo without this structure because of the low concentration of free Zn2+. PubMed: 14583199DOI: 10.1016/j.jmb.2003.09.008 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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