4bpf: Difference between revisions
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==High resolution crystal structure of Bacillus subtilis DltC S36A== | |||
<StructureSection load='4bpf' size='340' side='right'caption='[[4bpf]], [[Resolution|resolution]] 1.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bpf]] 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=4BPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BPF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.01Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4bpf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bpf OCA], [https://pdbe.org/4bpf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bpf RCSB], [https://www.ebi.ac.uk/pdbsum/4bpf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bpf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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;"> | |||
== 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<ref>PMID:26193422</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bpf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | |||
[[Category: Large Structures]] | |||
[[Category: Neumann P]] | |||
[[Category: Stubbs MT]] | |||
[[Category: Zimmermann S]] | |||
Latest revision as of 09:10, 15 November 2023
High resolution crystal structure of Bacillus subtilis DltC S36A
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