2pfy
From Proteopedia
(New page: 200px<br /><applet load="2pfy" size="350" color="white" frame="true" align="right" spinBox="true" caption="2pfy, resolution 1.950Å" /> '''Crystal structure o...) |
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==Overview== | ==Overview== | ||
| - | Gram-negative bacteria have developed several different transport systems | + | Gram-negative bacteria have developed several different transport systems for solute uptake. One of these, the tripartite ATP independent periplasmic transport system (TRAP-T), makes use of an extracytoplasmic solute receptor (ESR) which captures specific solutes with high affinity and transfers them to their partner permease complex located in the bacterial inner membrane. We hereby report the structures of DctP6 and DctP7, two such ESRs from Bordetella pertussis. These two proteins display a high degree of sequence and structural similarity and possess the "Venus flytrap" fold characteristic of ESRs, comprising two globular alpha/beta domains hinged together to form a ligand binding cleft. DctP6 and DctP7 both show a closed conformation due to the presence of one pyroglutamic acid molecule bound by highly conserved residues in their respective ligand binding sites. BLAST analyses have revealed that the DctP6 and DctP7 residues involved in ligand binding are strictly present in a number of predicted TRAP-T ESRs from other bacteria. In most cases, the genes encoding these TRAP-T systems are located in the vicinity of a gene coding for a pyroglutamic acid metabolising enzyme. Both the high degree of conservation of these ligand binding residues and the genomic context of these TRAP-T-coding operons in a number of bacterial species, suggest that DctP6 and DctP7 constitute the prototypes of a novel TRAP-T DctP subfamily involved in pyroglutamic acid transport. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal | + | Crystal structures of two Bordetella pertussis periplasmic receptors contribute to defining a novel pyroglutamic acid binding DctP subfamily., Rucktooa P, Antoine R, Herrou J, Huvent I, Locht C, Jacob-Dubuisson F, Villeret V, Bompard C, J Mol Biol. 2007 Jun 29;370(1):93-106. Epub 2007 Apr 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17499270 17499270] |
[[Category: Bordetella pertussis]] | [[Category: Bordetella pertussis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: tripartite atp independent periplasmic transport]] | [[Category: tripartite atp independent periplasmic transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:29:04 2008'' |
Revision as of 16:29, 21 February 2008
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Crystal structure of DctP7, a Bordetella pertussis extracytoplasmic solute receptor binding pyroglutamic acid
Overview
Gram-negative bacteria have developed several different transport systems for solute uptake. One of these, the tripartite ATP independent periplasmic transport system (TRAP-T), makes use of an extracytoplasmic solute receptor (ESR) which captures specific solutes with high affinity and transfers them to their partner permease complex located in the bacterial inner membrane. We hereby report the structures of DctP6 and DctP7, two such ESRs from Bordetella pertussis. These two proteins display a high degree of sequence and structural similarity and possess the "Venus flytrap" fold characteristic of ESRs, comprising two globular alpha/beta domains hinged together to form a ligand binding cleft. DctP6 and DctP7 both show a closed conformation due to the presence of one pyroglutamic acid molecule bound by highly conserved residues in their respective ligand binding sites. BLAST analyses have revealed that the DctP6 and DctP7 residues involved in ligand binding are strictly present in a number of predicted TRAP-T ESRs from other bacteria. In most cases, the genes encoding these TRAP-T systems are located in the vicinity of a gene coding for a pyroglutamic acid metabolising enzyme. Both the high degree of conservation of these ligand binding residues and the genomic context of these TRAP-T-coding operons in a number of bacterial species, suggest that DctP6 and DctP7 constitute the prototypes of a novel TRAP-T DctP subfamily involved in pyroglutamic acid transport.
About this Structure
2PFY is a Single protein structure of sequence from Bordetella pertussis with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structures of two Bordetella pertussis periplasmic receptors contribute to defining a novel pyroglutamic acid binding DctP subfamily., Rucktooa P, Antoine R, Herrou J, Huvent I, Locht C, Jacob-Dubuisson F, Villeret V, Bompard C, J Mol Biol. 2007 Jun 29;370(1):93-106. Epub 2007 Apr 25. PMID:17499270
Page seeded by OCA on Thu Feb 21 18:29:04 2008
