Metal Transport across Biomembranes: Emerging Models for a Distinct Chemistry

被引:75
作者
Argueello, Jose M. [1 ]
Raimunda, Daniel [1 ]
Gonzalez-Guerrero, Manuel [2 ]
机构
[1] Worcester Polytech Inst, Dept Chem & Biochem, Worcester, MA 01609 USA
[2] Univ Politecn Madrid, CBGP, Madrid 28223, Spain
基金
美国国家卫生研究院; 美国食品与农业研究所; 美国国家科学基金会;
关键词
ZINC TRANSPORTER; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; FUNCTIONAL ROLES; BINDING DOMAINS; COPPER; PROTEIN; ATPASES; CU+; RESISTANCE;
D O I
10.1074/jbc.R111.319343
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Transition metals are essential components of important biomolecules, and their homeostasis is central to many life processes. Transmembrane transporters are key elements controlling the distribution of metals in various compartments. However, due to their chemical properties, transition elements require transporters with different structural-functional characteristics from those of alkali and alkali earth ions. Emerging structural information and functional studies have revealed distinctive features of metal transport. Among these are the relevance of multifaceted events involving metal transfer among participating proteins, the importance of coordination geometry at transmembrane transport sites, and the presence of the largely irreversible steps associated with vectorial transport. Here, we discuss how these characteristics shape novel transition metal ion transport models.
引用
收藏
页码:13510 / 13517
页数:8
相关论文
共 83 条
[1]   Projection structure of the human copper transporter CTR1 at 6-A resolution reveals a compact trimer with a novel channel-like architecture [J].
Aller, SG ;
Unger, VM .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2006, 103 (10) :3627-3632
[2]  
[Anonymous], 2001, BIOL CHEM ELEMENTS
[3]   Characteristics of zinc transport by two bacterial cation diffusion facilitators from Ralstonia metallidurans CH34 and Escherichia coli [J].
Anton, A ;
Weltrowski, A ;
Haney, CJ ;
Franke, S ;
Grass, G ;
Rensing, C ;
Nies, DH .
JOURNAL OF BACTERIOLOGY, 2004, 186 (22) :7499-7507
[4]   Identification of ion-selectivity determinants in heavy-metal transport P1B-type ATPases [J].
Argüello, JM .
JOURNAL OF MEMBRANE BIOLOGY, 2003, 195 (02) :93-108
[5]   The structure and function of heavy metal transport P1B-ATPases [J].
Arguello, Jose M. ;
Eren, Elif ;
Gonzalez-Guerrero, Manuel .
BIOMETALS, 2007, 20 (3-4) :233-248
[6]   Metallochaperones and metal-transporting ATPases: A comparative analysis of sequences and structures [J].
Arnesano, F ;
Banci, L ;
Bertini, I ;
Ciofi-Baffoni, S ;
Molteni, E ;
Huffman, DL ;
O'Halloran, TV .
GENOME RESEARCH, 2002, 12 (02) :255-271
[7]   Direct Metal Transfer between Periplasmic Proteins Identifies a Bacterial Copper Chaperone [J].
Bagai, Ireena ;
Rensing, Christopher ;
Blackburn, Ninian J. ;
McEvoy, Megan M. .
BIOCHEMISTRY, 2008, 47 (44) :11408-11414
[8]   Substrate-linked conformational change in the periplasmic component of a Cu(I)/Ag(I) efflux system [J].
Bagai, Ireena ;
Liu, Wenbo ;
Rensing, Christopher ;
Blackburn, Ninian J. ;
McEvoy, Megan M. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (49) :35695-35702
[9]   Electrostatics of nanosystems: Application to microtubules and the ribosome [J].
Baker, NA ;
Sept, D ;
Joseph, S ;
Holst, MJ ;
McCammon, JA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (18) :10037-10041
[10]   The Lumenal Loop Met672-Pro707 of Copper-transporting ATPase ATP7A Binds Metals and Facilitates Copper Release from the Intramembrane Sites [J].
Barry, Amanda N. ;
Otoikhian, Adenike ;
Bhatt, Sujata ;
Shinde, Ujwal ;
Tsivkovskii, Ruslan ;
Blackburn, Ninian J. ;
Lutsenko, Svetlana .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2011, 286 (30) :26585-26594