#!/usr/bin/perl # use module use XML::Simple; use Data::Dumper; # create object $xml = new XML::Simple (KeyAttr=>[]); #read XML file $data = $xml->XMLin("data.xml"); #dereference hash ref #print Dumper($data); print $data->{PMID}, "\n"; print $data->{Article}->{ArticleTitle}, "\n"; foreach $e (@{$data->{Article}->{AuthorList}->{Author}}) { $authors.= $e->{LastName}." ".$e->{Initials}.', '; } print $data->{Article}->{Journal}->{ISOAbbreviation}, " "; print $data->{Article}->{Journal}->{JournalIssue}->{PubDate}->{Year}, ";", ; print $data->{Article}->{Journal}->{JournalIssue}->{Volume}, ":"; print $data->{Article}->{Pagination}->{MedlinePgn}, "." ; print "\n"; #### 1766380
5 9 1991 Sep Mol. Microbiol. PhoP/PhoQ: macrophage-specific modulators of Salmonella virulence? 2073-8 Miller S I SI Tsirigos K T KT Dinous A E AE
16039843 2005 08 01 2005 12 08 2006 11 15
0959-440X 15 4 2005 Aug Current opinion in structural biology Curr. Opin. Struct. Biol. TonB-dependent outer membrane transport: going for Baroque? 394-400 The import of essential organometallic micronutrients (such as iron-siderophores and vitamin B(12)) across the outer membrane of Gram-negative bacteria proceeds via TonB-dependent outer membrane transporters (TBDTs). The TBDT couples to the TonB protein, which is part of a multiprotein complex in the plasma (inner) membrane. Five crystal structures of TBDTs illustrate clearly the architecture of the protein in energy-independent substrate-free and substrate-bound states. In each of the TBDT structures, an N-terminal hatch (or plug or cork) domain occludes the lumen of a 22-stranded beta barrel. The manner by which substrate passes through the transporter (the "hatch-barrel problem") is currently unknown. Solution NMR and X-ray crystallographic structures of various TonB domains indicate a striking structural plasticity of this protein. Thermodynamic, biochemical and bacteriological studies of TonB and TBDTs indicate further that existing structures do not yet capture critical energy-dependent and in vivo conformations of the transport cycle. The reconciliation of structural and non-structural experimental data, and the unambiguous experimental elucidation of a detailed molecular mechanism of transport are current challenges for this field. Department of Molecular Physiology and Biological Physics, University of Virginia, PO Box 800736, Charlottesville, VA 22908-0736, USA. mwiener@virginia.edu Wiener Michael C MC eng DK 59999 DK NIDDK Journal Article Research Support, N.I.H., Extramural Research Support, U.S. Gov't, P.H.S. Review
England Curr Opin Struct Biol 9107784 0 Bacterial Outer Membrane Proteins 0 Bacterial Proteins 0 Membrane Proteins 0 Multiprotein Complexes 0 tonB protein, Bacteria IM Bacterial Outer Membrane Proteins chemistry metabolism Bacterial Proteins chemistry metabolism Biological Transport physiology Crystallography, X-Ray Membrane Proteins chemistry metabolism Models, Molecular Multiprotein Complexes Protein Conformation 38
2005 6 7 2005 6 18 2005 7 8 2005 7 26 9 0 2005 12 13 9 0 ppublish S0959-440X(05)00124-7 10.1016/j.sbi.2005.07.001 16039843