Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2 Pt 1
pubmed:dateCreated
2003-1-27
pubmed:abstractText
RD1 is a 7-kDa globular protein from the Antarctic eel pout Lycodichthys dearborni. It belongs to type III of the four types of antifreeze proteins (AFPs) found in marine fishes living at subzero temperatures. For type III AFP, a potential ice-binding flat surface has been identified and is imbedded with side chains capable of making hydrogen bonds with a specific lattice plane on ice. So far, all crystallographic studies on type III AFPs were carried out using the Atlantic ocean pout Macrozoarces americanus as the source organism. Here we present the crystal structure of a type III AFP from a different zoarcid fish, and at an ultra-high resolution of 0.62 A. The protein fold of RD1 comprises a compact globular domain with two internal tandem motifs arranged about a pseudo-dyad symmetry. Each motif of the "pretzel fold" includes four short beta-strands and a 3(10) helix. There is a novel internal cavity of 45 A(3) surrounded by eight conserved nonpolar residues. The model contains several residues with alternate conformations, and a number of split water molecules, probably caused by alternate interactions with the protein molecule. After extensive refinement that includes hydrogen atoms, significant residual electron densities associated with the electrons of peptides and many other bonds could be visualized.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-10207002, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-10737790, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-11162099, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-11237011, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-11504613, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-1758883, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-2752054, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-2851724, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-3403560, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-5700707, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-7020376, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-7696304, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-8433969, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-8438165, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-8918883, http://linkedlifedata.com/resource/pubmed/commentcorrection/12547803-9591641
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3495
pubmed:author
pubmed:issnType
Print
pubmed:volume
84
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1228-37
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:12547803-Amino Acid Sequence, pubmed-meshheading:12547803-Animals, pubmed-meshheading:12547803-Antifreeze Proteins, Type III, pubmed-meshheading:12547803-Computer Simulation, pubmed-meshheading:12547803-Databases, Protein, pubmed-meshheading:12547803-Eels, pubmed-meshheading:12547803-Macromolecular Substances, pubmed-meshheading:12547803-Magnetic Resonance Spectroscopy, pubmed-meshheading:12547803-Models, Molecular, pubmed-meshheading:12547803-Molecular Sequence Data, pubmed-meshheading:12547803-Protein Conformation, pubmed-meshheading:12547803-Protein Folding, pubmed-meshheading:12547803-Protein Structure, Tertiary, pubmed-meshheading:12547803-Quality Control, pubmed-meshheading:12547803-Solvents, pubmed-meshheading:12547803-Species Specificity, pubmed-meshheading:12547803-Water, pubmed-meshheading:12547803-X-Ray Diffraction
pubmed:year
2003
pubmed:articleTitle
The refined crystal structure of an eel pout type III antifreeze protein RD1 at 0.62-A resolution reveals structural microheterogeneity of protein and solvation.
pubmed:affiliation
Institute of Biological Chemistry, Academia Sinica, Taipei 11529, Taiwan.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Evaluation Studies, Validation Studies