View source for 5zws


==Crystal structure of apo-acyl carrier protein from Leishmania major==
<StructureSection load='5zws' size='340' side='right'caption='[[5zws]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zws]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZWS 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]] 2&#8491;</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=5zws FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zws OCA], [https://pdbe.org/5zws PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zws RCSB], [https://www.ebi.ac.uk/pdbsum/5zws PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zws ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E9AD06_LEIMA E9AD06_LEIMA] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU000722]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Acyl carrier proteins (ACPs) play crucial roles in the biosynthesis of fatty acids, non-ribosomal polypeptides and polyketides. The three-dimensional NMR structure of Leishmania major holo-LmACP, belonging to the type II pathway, has been reported previously, but the structure of its apo-form and its conformational differences with the holo-form remain to be explored. Here we report the crystal structures of apo-LmACP (wild-type and S37A mutant) at 2.0A resolution and compare their key features with the structures of holo-LmACP (wild-type) and other type II ACPs from Escherichia coli and Plasmodium falciparum. The crystal structure of apo-LmACP, which is homologous to other type II ACPs, displays some key structural rearrangements as compared to its holo-structure. Contrary to holo-form, which exists predominantly as a monomer, the apo-form exists as a mixture of monomeric and dimeric population in solution. In contrast to the closed structure of apo-LmACP, holo-LmACP structure was observed in an open conformation as a result of reorganization of specific helices and loops. We propose that the structural changes exhibited by LmACP occur due to the attachment of the phosphopantetheine arm and may be a prerequisite for the initiation of fatty acid synthesis. The movement of helix 3 may also play a role in the dissociation of holo-LmACP from its cognate enzymes of the FAS II pathway.

A conformational switch from a closed apo- to an open holo-form equips the acyl carrier protein for acyl chain accommodation.,Arya R, Sharma B, Dhembla C, Pal RK, Patel AK, Sundd M, Ghosh B, Makde RD, Kundu S Biochim Biophys Acta Proteins Proteom. 2018 Dec 10;1867(3):163-174. doi:, 10.1016/j.bbapap.2018.12.001. PMID:30543875<ref>PMID:30543875</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zws" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Leishmania major]]
[[Category: Arya R]]
[[Category: Kundu S]]
[[Category: Makde RD]]
[[Category: Sharma B]]