6lvt: Difference between revisions
New page: '''Unreleased structure''' The entry 6lvt is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Solution structure of holo acyl carrier protein from Thermotoga maritima== | ||
<StructureSection load='6lvt' size='340' side='right'caption='[[6lvt]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6lvt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LVT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6LVT FirstGlance]. <br> | |||
</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=6lvt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lvt OCA], [https://pdbe.org/6lvt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6lvt RCSB], [https://www.ebi.ac.uk/pdbsum/6lvt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6lvt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ACP_THEMA ACP_THEMA] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[HAMAP-Rule:MF_01217] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Thermotoga maritima, a deep-branching hyperthermophilic bacterium, expresses an extraordinarily stable Thermotoga maritima acyl carrier protein (Tm-ACP) that functions as a carrier in the fatty acid synthesis system at near-boiling aqueous environments. Here, to understand the hyperthermal adaptation of Tm-ACP, we investigated the structure and dynamics of Tm-ACP by nuclear magnetic resonance (NMR) spectroscopy. The melting temperature of Tm-ACP (101.4 degrees C) far exceeds that of other ACPs, owing to extensive ionic interactions and tight hydrophobic packing. The D59 residue, which replaces Pro/Ser of other ACPs, mediates ionic clustering between helices III and IV. This creates a wide pocket entrance to facilitate the accommodation of long acyl chains required for hyperthermal adaptation of the T. maritima cell membrane. Tm-ACP is revealed to be the first ACP that harbor an amide proton hyperprotected against hydrogen/deuterium exchange for I15. The hydrophobic interactions mediated by I15 appear to be the key driving forces of the global folding process of Tm-ACP. Our findings provide insights into the structural basis of the hyperthermal adaptation of ACP, which might have allowed T. maritima to survive in hot ancient oceans. | |||
Structural Characterization of an ACP from Thermotoga maritima: Insights into Hyperthermal Adaptation.,Lee Y, Jang A, Jeong MC, Park N, Park J, Lee WC, Cheong C, Kim Y Int J Mol Sci. 2020 Apr 9;21(7). pii: ijms21072600. doi: 10.3390/ijms21072600. PMID:32283632<ref>PMID:32283632</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6lvt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Thermotoga maritima MSB8]] | |||
[[Category: Kim Y]] | |||
[[Category: Lee Y]] | |||