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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
31
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pubmed:dateCreated |
2000-9-7
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pubmed:databankReference |
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pubmed:abstractText |
ZipA, an essential component of cell division in Escherichia coli, interacts with the FtsZ protein at the midcell in one of the initial steps of septum formation. The high-resolution solution structure of the 144-residue C-terminal domain of E. coli ZipA (ZipA(185)(-)(328)) has been determined by multidimensional heteronuclear NMR. A total of 30 structures were calculated by means of hybrid distance geometry-simulated annealing using a total of 2758 experimental NMR restraints. The atomic root means square distribution about the mean coordinate positions for residues 6-142 for the 30 structures is 0.37 +/- 0.04 A for the backbone atoms, 0. 78 +/- 0.05 A for all atoms, and 0.45 +/- 0.04 A for all atoms excluding disordered side chains. The NMR solution structure of ZipA(185)(-)(328) is composed of three alpha-helices and a beta-sheet consisting of six antiparallel beta-strands where the alpha-helices and the beta-sheet form surfaces directly opposite each other. A C-terminal peptide from FtsZ has been shown to bind ZipA(185)(-)(328) in a hydrophobic channel formed by the beta-sheet providing insight into the ZipA-FtsZ interaction. An unexpected similarity between the ZipA(185)(-)(328) fold and the split beta-alpha-beta fold observed in many RNA binding proteins may further our understanding of the critical ZipA-FtsZ interaction.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FtsZ protein, Bacteria,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Solutions,
http://linkedlifedata.com/resource/pubmed/chemical/ZipA protein, E coli
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
39
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
9146-56
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:10924108-Amino Acid Sequence,
pubmed-meshheading:10924108-Bacterial Proteins,
pubmed-meshheading:10924108-Carrier Proteins,
pubmed-meshheading:10924108-Cell Cycle Proteins,
pubmed-meshheading:10924108-Cell Division,
pubmed-meshheading:10924108-Computer Simulation,
pubmed-meshheading:10924108-Crystallography, X-Ray,
pubmed-meshheading:10924108-Cytoskeletal Proteins,
pubmed-meshheading:10924108-Escherichia coli,
pubmed-meshheading:10924108-Escherichia coli Proteins,
pubmed-meshheading:10924108-Models, Molecular,
pubmed-meshheading:10924108-Molecular Sequence Data,
pubmed-meshheading:10924108-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:10924108-Peptide Fragments,
pubmed-meshheading:10924108-Protein Folding,
pubmed-meshheading:10924108-Protein Structure, Secondary,
pubmed-meshheading:10924108-RNA-Binding Proteins,
pubmed-meshheading:10924108-Solutions
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pubmed:year |
2000
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pubmed:articleTitle |
Solution structure of ZipA, a crucial component of Escherichia coli cell division.
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pubmed:affiliation |
Department of Biological Chemistry, Wyeth Research, Cambridge, Massachusetts 02140, USA.
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pubmed:publicationType |
Journal Article
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