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| | <StructureSection load='4bph' size='340' side='right'caption='[[4bph]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='4bph' size='340' side='right'caption='[[4bph]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4bph]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BPH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BPH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4bph]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BPH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</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]] 1.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bpf|4bpf]], [[4bpg|4bpg]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PNS:4-PHOSPHOPANTETHEINE'>PNS</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/D-alanine--poly(phosphoribitol)_ligase D-alanine--poly(phosphoribitol) ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.13 6.1.1.13] </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=4bph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bph OCA], [https://pdbe.org/4bph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bph RCSB], [https://www.ebi.ac.uk/pdbsum/4bph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bph ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bph OCA], [http://pdbe.org/4bph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bph RCSB], [http://www.ebi.ac.uk/pdbsum/4bph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bph ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DLTC_BACSU DLTC_BACSU]] Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Activated D-alanyl-Dcp donates its D-alanyl substituent to membrane-associated LTA. | + | [https://www.uniprot.org/uniprot/DLTC_BACSU DLTC_BACSU] Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Activated D-alanyl-Dcp donates its D-alanyl substituent to membrane-associated LTA. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Vibrio subtilis ehrenberg 1835]] | + | [[Category: Bacillus subtilis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Neumann, P]] | + | [[Category: Neumann P]] |
| - | [[Category: Stubbs, M T]] | + | [[Category: Stubbs MT]] |
| - | [[Category: Zimmermann, S]] | + | [[Category: Zimmermann S]] |
| - | [[Category: Acyl-carrier-protein]]
| + | |
| - | [[Category: D-alanylation]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Lipoteichoic acid]]
| + | |
| - | [[Category: Peptidyl-carrier-protein]]
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| Structural highlights
Function
DLTC_BACSU Involved in the biosynthesis of D-alanyl-lipoteichoic acid (LTA). Activated D-alanyl-Dcp donates its D-alanyl substituent to membrane-associated LTA.
Publication Abstract from PubMed
d-Alanylation of lipoteichoic acids plays an important role in modulating the properties of Gram-positive bacteria cell walls. The d-alanyl carrier protein DltC from Bacillus subtilis has been solved in apo- and two cofactor-modified holo-forms, whereby the entire phosphopantetheine moiety is defined in one. The atomic resolution of the apo-structure allows delineation of alternative conformations within the hydrophobic core of the 78 residue four helix bundle. In contrast to previous reports for a peptidyl carrier protein from a non-ribosomal peptide synthetase, no obvious structural differences between apo- and holo-DltC forms are observed. Solution NMR spectroscopy confirms these findings and demonstrates in addition that the two forms exhibit similar backbone dynamics on the ps-ns and ms timescales.
High-resolution structures of the d-alanyl carrier protein (Dcp) DltC from Bacillus subtilis reveal equivalent conformations of apo- and holo-forms.,Zimmermann S, Pfennig S, Neumann P, Yonus H, Weininger U, Kovermann M, Balbach J, Stubbs MT FEBS Lett. 2015 Jul 17. pii: S0014-5793(15)00587-6. doi:, 10.1016/j.febslet.2015.07.008. PMID:26193422[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Zimmermann S, Pfennig S, Neumann P, Yonus H, Weininger U, Kovermann M, Balbach J, Stubbs MT. High-resolution structures of the d-alanyl carrier protein (Dcp) DltC from Bacillus subtilis reveal equivalent conformations of apo- and holo-forms. FEBS Lett. 2015 Jul 17. pii: S0014-5793(15)00587-6. doi:, 10.1016/j.febslet.2015.07.008. PMID:26193422 doi:http://dx.doi.org/10.1016/j.febslet.2015.07.008
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