View source for 8hcz


==N-terminal domain structure of mycobacterium tuberculosis FadD23==
<StructureSection load='8hcz' size='340' side='right'caption='[[8hcz]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8hcz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HCZ 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]] 1.48&#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=8hcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hcz OCA], [https://pdbe.org/8hcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hcz RCSB], [https://www.ebi.ac.uk/pdbsum/8hcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hcz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FAA23_MYCTU FAA23_MYCTU] Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase (PKS) type III for further chain extension (Probable). Involved in the biosynthesis of sulfolipid 1 (SL-1) (PubMed:17389997, PubMed:17768256).<ref>PMID:17389997</ref> <ref>PMID:17768256</ref> <ref>PMID:17768256</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sulfolipid-1 (SL-1) is located in the Mycobacterium tuberculosis (M. tb) cell wall, and is essential for pathogen virulence and intracellular growth. Multiple proteins (e.g., Pks2, FadD23, PapA1, and MmpL8) in the SL-1 synthesis pathway can be treated as drug targets, but, to date, their structures have not been solved. The crystal structures of FadD23 bound to ATP or hexadecanoyl adenylate was determined in this study. We have also investigated long-chain saturated fatty acids as biological substrates of FadD23 through structural, biological, and chemical analyses. The mutation at the active site of FadD23 greatly influences enzymatic activity. Meanwhile, the FadD23 N-terminal domain alone cannot bind palmitic acid without C-terminal domain facilitation since it is almost inactive after removing the C-terminal domain. FadD23 is the first protein in the SL-1 synthesis pathway whose structure has been solved. These results reveal the importance of the C-terminal domain in the catalytic mechanism.

The Key Roles of Mycobacterium tuberculosis FadD23 C-terminal Domain in Catalytic Mechanisms.,Yan M, Cao L, Zhao L, Zhou W, Liu X, Zhang W, Rao Z Front Microbiol. 2023 Feb 21;14:1090534. doi: 10.3389/fmicb.2023.1090534. , eCollection 2023. PMID:36896429<ref>PMID:36896429</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8hcz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis H37Rv]]
[[Category: Liu X]]
[[Category: Rao ZH]]
[[Category: Yan MR]]
[[Category: Zhang W]]