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| | <StructureSection load='2hzl' size='340' side='right'caption='[[2hzl]], [[Resolution|resolution]] 1.40Å' scene=''> | | <StructureSection load='2hzl' size='340' side='right'caption='[[2hzl]], [[Resolution|resolution]] 1.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hzl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhos4 Rhos4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HZL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hzl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides_2.4.1 Cereibacter sphaeroides 2.4.1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HZL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hzk|2hzk]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hzl OCA], [https://pdbe.org/2hzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hzl RCSB], [https://www.ebi.ac.uk/pdbsum/2hzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hzl ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hzl OCA], [https://pdbe.org/2hzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hzl RCSB], [https://www.ebi.ac.uk/pdbsum/2hzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hzl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TAKP_RHOS4 TAKP_RHOS4]] Part of the tripartite ATP-independent periplasmic (TRAP) transport system TakPQM involved in the uptake of alpha-keto acids. This protein specifically binds alpha-keto acids including pyruvate, oxobutyrate, oxovalerate and 4-methyl-2-oxovalerate. Ligand-binding affinity increases with the increasing chain length of the aliphatic backbone of the ligand. Is not able to bind alpha-ketoglutarate.[UniProtKB:P44542]<ref>PMID:17362499</ref>
| + | [https://www.uniprot.org/uniprot/TAKP_CERS4 TAKP_CERS4] Part of the tripartite ATP-independent periplasmic (TRAP) transport system TakPQM involved in the uptake of alpha-keto acids. This protein specifically binds alpha-keto acids including pyruvate, oxobutyrate, oxovalerate and 4-methyl-2-oxovalerate. Ligand-binding affinity increases with the increasing chain length of the aliphatic backbone of the ligand. Is not able to bind alpha-ketoglutarate.[UniProtKB:P44542]<ref>PMID:17362499</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Cereibacter sphaeroides 2 4.1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Rhos4]]
| + | [[Category: Alonso B]] |
| - | [[Category: Alonso, B]] | + | [[Category: Arnoux P]] |
| - | [[Category: Arnoux, P]] | + | [[Category: Gonin S]] |
| - | [[Category: Gonin, S]] | + | [[Category: Pierru B]] |
| - | [[Category: Pierru, B]] | + | [[Category: Pignol D]] |
| - | [[Category: Pignol, D]] | + | [[Category: Sabaty M]] |
| - | [[Category: Sabaty, M]] | + | |
| - | [[Category: Ligand binding]]
| + | |
| - | [[Category: Periplasmic subunit]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Trap transporter]]
| + | |
| Structural highlights
Function
TAKP_CERS4 Part of the tripartite ATP-independent periplasmic (TRAP) transport system TakPQM involved in the uptake of alpha-keto acids. This protein specifically binds alpha-keto acids including pyruvate, oxobutyrate, oxovalerate and 4-methyl-2-oxovalerate. Ligand-binding affinity increases with the increasing chain length of the aliphatic backbone of the ligand. Is not able to bind alpha-ketoglutarate.[UniProtKB:P44542][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
BACKGROUND: The import of solutes into the bacterial cytoplasm involves several types of membrane transporters, which may be driven by ATP hydrolysis (ABC transporters) or by an ion or H+ electrochemical membrane potential, as in the tripartite ATP-independent periplasmic system (TRAP). In both the ABC and TRAP systems, a specific periplasmic protein from the ESR family (Extracytoplasmic Solute Receptors) is often involved for the recruitment of the solute and its presentation to the membrane complex. In Rhodobacter sphaeroides, TakP (previously named SmoM) is an ESR from a TRAP transporter and binds alpha-keto acids in vitro. RESULTS: We describe the high-resolution crystal structures of TakP in its unliganded form and as a complex with sodium-pyruvate. The results show a limited "Venus flytrap" conformational change induced by substrate binding. In the liganded structure, a cation (most probably a sodium ion) is present and plays a key role in the association of the pyruvate to the protein. The structure of the binding pocket gives a rationale for the relative affinities of various ligands that were tested from a fluorescence assay. The protein appears to be dimeric in solution and in the crystals, with a helix-swapping structure largely participating in the dimer formation. A 30 A-long water channel buried at the dimer interface connects the two ligand binding cavities of the dimer. CONCLUSION: The concerted recruitment by TakP of the substrate group with a cation could represent a first step in the coupled transport of both partners, providing the driving force for solute import. Furthermore, the unexpected dimeric structure of TakP suggests a molecular mechanism of solute uptake by the dimeric ESR via a channel that connects the binding sites of the two monomers.
Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding.,Gonin S, Arnoux P, Pierru B, Lavergne J, Alonso B, Sabaty M, Pignol D BMC Struct Biol. 2007 Mar 15;7:11. PMID:17362499[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gonin S, Arnoux P, Pierru B, Lavergne J, Alonso B, Sabaty M, Pignol D. Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding. BMC Struct Biol. 2007 Mar 15;7:11. PMID:17362499 doi:10.1186/1472-6807-7-11
- ↑ Gonin S, Arnoux P, Pierru B, Lavergne J, Alonso B, Sabaty M, Pignol D. Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding. BMC Struct Biol. 2007 Mar 15;7:11. PMID:17362499 doi:10.1186/1472-6807-7-11
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