2ogw
From Proteopedia
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Structure of ABC type zinc transporter from E. coli
Overview
ATP-binding cassette superfamily of periplasmic metal transporters are, known to be vital for maintaining ion homeostasis in several pathogenic, and non-pathogenic bacteria. We have determined crystal structure of the, high-affinity zinc transporter ZnuA from Escherichia coli at 1.8 A, resolution. This structure represents the first native (non-recombinant), protein structure of a periplasmic metal binding protein. ZnuA reveals, numerous conformational features, which occur either in Zn(2+) or in, Mn(2+) transporters, and presents a unique conformational state. A, comprehensive comparison of ZnuA with other periplasmic ligand binding, protein structures suggests vital mechanistic differences between bound, and release states of metal transporters. The key new attributes in ZnuA, include a C-domain disulfide bond, an extra alpha-helix proximal to the, highly charged metal chelating mobile loop region, alternate conformations, of secondary shell stabilizing residues at the metal binding site, and, domain movements potentially controlled by salt bridges. Based on in-depth, structural analyses of five metal binding transporters, we present here a, mechanistic model termed as "partial domain slippage" for binding and, release of Zn(2+).
About this Structure
2OGW is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structural Analysis of ABC-family Periplasmic Zinc Binding Protein Provides New Insights Into Mechanism of Ligand Uptake and Release., Chandra BR, Yogavel M, Sharma A, J Mol Biol. 2007 Jan 23;. PMID:17306297
Page seeded by OCA on Wed Nov 21 13:10:31 2007
Categories: Escherichia coli | Single protein | Sharma, A. | Yogavel, M. | ZN | Abc | Transporter | Zinc
