NMR structure of lipoprotein YxeF from Bacillus subtilis reveals a calycin fold and distant homology with the lipocalin Blc from Escherichia coli.
The soluble monomeric domain of lipoprotein YxeF from the Gram positive bacterium B. subtilis was selected by the Northeast Structural Genomics Consortium (NESG) as a target of a biomedical theme project focusing on the structure determination of the soluble domains of bacterial lipoproteins. The so...
| Main Authors: | , , , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2012-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3367933?pdf=render |
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| author | Yibing Wu Marco Punta Rong Xiao Thomas B Acton Bharathwaj Sathyamoorthy Fabian Dey Markus Fischer Arne Skerra Burkhard Rost Gaetano T Montelione Thomas Szyperski |
| author_facet | Yibing Wu Marco Punta Rong Xiao Thomas B Acton Bharathwaj Sathyamoorthy Fabian Dey Markus Fischer Arne Skerra Burkhard Rost Gaetano T Montelione Thomas Szyperski |
| author_sort | Yibing Wu |
| collection | DOAJ |
| description | The soluble monomeric domain of lipoprotein YxeF from the Gram positive bacterium B. subtilis was selected by the Northeast Structural Genomics Consortium (NESG) as a target of a biomedical theme project focusing on the structure determination of the soluble domains of bacterial lipoproteins. The solution NMR structure of YxeF reveals a calycin fold and distant homology with the lipocalin Blc from the Gram-negative bacterium E.coli. In particular, the characteristic β-barrel, which is open to the solvent at one end, is extremely well conserved in YxeF with respect to Blc. The identification of YxeF as the first lipocalin homologue occurring in a Gram-positive bacterium suggests that lipocalins emerged before the evolutionary divergence of Gram positive and Gram negative bacteria. Since YxeF is devoid of the α-helix that packs in all lipocalins with known structure against the β-barrel to form a second hydrophobic core, we propose to introduce a new lipocalin sub-family named 'slim lipocalins', with YxeF and the other members of Pfam family PF11631 to which YxeF belongs constituting the first representatives. The results presented here exemplify the impact of structural genomics to enhance our understanding of biology and to generate new biological hypotheses. |
| first_indexed | 2024-04-13T16:14:58Z |
| format | Article |
| id | doaj.art-75854a80aed04bf4a7b9adb71cf253d4 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-04-13T16:14:58Z |
| publishDate | 2012-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-75854a80aed04bf4a7b9adb71cf253d42022-12-22T02:40:05ZengPublic Library of Science (PLoS)PLoS ONE1932-62032012-01-0176e3740410.1371/journal.pone.0037404NMR structure of lipoprotein YxeF from Bacillus subtilis reveals a calycin fold and distant homology with the lipocalin Blc from Escherichia coli.Yibing WuMarco PuntaRong XiaoThomas B ActonBharathwaj SathyamoorthyFabian DeyMarkus FischerArne SkerraBurkhard RostGaetano T MontelioneThomas SzyperskiThe soluble monomeric domain of lipoprotein YxeF from the Gram positive bacterium B. subtilis was selected by the Northeast Structural Genomics Consortium (NESG) as a target of a biomedical theme project focusing on the structure determination of the soluble domains of bacterial lipoproteins. The solution NMR structure of YxeF reveals a calycin fold and distant homology with the lipocalin Blc from the Gram-negative bacterium E.coli. In particular, the characteristic β-barrel, which is open to the solvent at one end, is extremely well conserved in YxeF with respect to Blc. The identification of YxeF as the first lipocalin homologue occurring in a Gram-positive bacterium suggests that lipocalins emerged before the evolutionary divergence of Gram positive and Gram negative bacteria. Since YxeF is devoid of the α-helix that packs in all lipocalins with known structure against the β-barrel to form a second hydrophobic core, we propose to introduce a new lipocalin sub-family named 'slim lipocalins', with YxeF and the other members of Pfam family PF11631 to which YxeF belongs constituting the first representatives. The results presented here exemplify the impact of structural genomics to enhance our understanding of biology and to generate new biological hypotheses.http://europepmc.org/articles/PMC3367933?pdf=render |
| spellingShingle | Yibing Wu Marco Punta Rong Xiao Thomas B Acton Bharathwaj Sathyamoorthy Fabian Dey Markus Fischer Arne Skerra Burkhard Rost Gaetano T Montelione Thomas Szyperski NMR structure of lipoprotein YxeF from Bacillus subtilis reveals a calycin fold and distant homology with the lipocalin Blc from Escherichia coli. PLoS ONE |
| title | NMR structure of lipoprotein YxeF from Bacillus subtilis reveals a calycin fold and distant homology with the lipocalin Blc from Escherichia coli. |
| title_full | NMR structure of lipoprotein YxeF from Bacillus subtilis reveals a calycin fold and distant homology with the lipocalin Blc from Escherichia coli. |
| title_fullStr | NMR structure of lipoprotein YxeF from Bacillus subtilis reveals a calycin fold and distant homology with the lipocalin Blc from Escherichia coli. |
| title_full_unstemmed | NMR structure of lipoprotein YxeF from Bacillus subtilis reveals a calycin fold and distant homology with the lipocalin Blc from Escherichia coli. |
| title_short | NMR structure of lipoprotein YxeF from Bacillus subtilis reveals a calycin fold and distant homology with the lipocalin Blc from Escherichia coli. |
| title_sort | nmr structure of lipoprotein yxef from bacillus subtilis reveals a calycin fold and distant homology with the lipocalin blc from escherichia coli |
| url | http://europepmc.org/articles/PMC3367933?pdf=render |
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