Source:http://linkedlifedata.com/resource/pubmed/id/21153711
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2011-5-9
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pubmed:abstractText |
The conserved Lipoprotein-17 domain of membrane-associated protein Q9PRA0_UREPA from Ureaplasma parvum was selected for structure determination by the Northeast Structural Genomics Consortium, as part of the Protein Structure Initiative's program on structure-function analysis of protein domains from large domain sequence families lacking structural representatives. The 100-residue Lipoprotein-17 domain is a "domain of unknown function" (DUF) that is a member of Pfam protein family PF04200, a large domain family for which no members have characterized biochemical functions. The three-dimensional structure of the Lipoprotein-17 domain of protein Q9PRA0_UREPA was determined by both solution NMR and by X-ray crystallography at 2.5 Å. The two structures are in good agreement with each other. The domain structure features three ?-helices, ?1 through ?3, and five ?-strands. Strands ?1/?2, ?3/?4, ?4/?5 are anti-parallel to each other. Strands ?1and ?2 are orthogonal to strands ?3, ?4, ?5, while helix ?3 is formed between the strands ?3 and ?4. One-turn helix ?2 is formed between the strands ?1 and ?2, while helix ?1 occurs in the N-terminal polypeptide segment. Searches of the Protein Data Bank do not identify any other protein with significant structural similarity to Lipoprotein-17 domain of Q9PRA0_UREPA, indicating that it is a novel protein fold.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1570-0267
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pubmed:author |
pubmed-author:ActonThomas BTB,
pubmed-author:CiccosantiColleenC,
pubmed-author:EverettJohn KJK,
pubmed-author:JanjuaHaleemaH,
pubmed-author:ManiRajeswariR,
pubmed-author:MoaGG,
pubmed-author:MontelioneGaetano TGT,
pubmed-author:NeelyHelenH,
pubmed-author:RongXiaoX,
pubmed-author:SwapnaG V TGV,
pubmed-author:VorobievSergeyS
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pubmed:issnType |
Electronic
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
27-32
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pubmed:meshHeading |
pubmed-meshheading:21153711-Amino Acid Sequence,
pubmed-meshheading:21153711-Crystallography, X-Ray,
pubmed-meshheading:21153711-Lipoproteins,
pubmed-meshheading:21153711-Membrane Proteins,
pubmed-meshheading:21153711-Models, Molecular,
pubmed-meshheading:21153711-Molecular Sequence Data,
pubmed-meshheading:21153711-Mycoplasma,
pubmed-meshheading:21153711-Nuclear Magnetic Resonance, Biomolecular,
pubmed-meshheading:21153711-Protein Conformation,
pubmed-meshheading:21153711-Protein Folding,
pubmed-meshheading:21153711-Protein Structure, Tertiary,
pubmed-meshheading:21153711-Solutions,
pubmed-meshheading:21153711-Ureaplasma
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pubmed:year |
2011
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pubmed:articleTitle |
Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.
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pubmed:affiliation |
Center for Advanced Biotechnology and Medicine, Department of Molecular Biology and Biochemistry, Rutgers, The State University of New Jersey, Piscataway, 08854, USA.
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pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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