View source for 4bpf


==High resolution crystal structure of Bacillus subtilis DltC S36A==
<StructureSection load='4bpf' size='340' side='right'caption='[[4bpf]], [[Resolution|resolution]] 1.01&Aring;' 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]] 1.01&#8491;</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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bpf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Neumann P]]
[[Category: Stubbs MT]]
[[Category: Zimmermann S]]