8cv1: Difference between revisions

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'''Unreleased structure'''


The entry 8cv1 is ON HOLD  until Paper Publication
==ACP1-KS-AT domains of mycobacterial Pks13==
<StructureSection load='8cv1' size='340' side='right'caption='[[8cv1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8cv1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CV1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.6&#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=8cv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cv1 OCA], [https://pdbe.org/8cv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cv1 RCSB], [https://www.ebi.ac.uk/pdbsum/8cv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cv1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/I7FMV0_MYCS2 I7FMV0_MYCS2]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The mycolic acid layer of the Mycobacterium tuberculosis cell wall is essential for viability and virulence, and the enzymes responsible for its synthesis are targets for antimycobacterial drug development. Polyketide synthase 13 (Pks13) is a module encoding several enzymatic and transport functions that carries out the condensation of two different long-chain fatty acids to produce mycolic acids. We determined structures by cryogenic-electron microscopy of dimeric multi-enzyme Pks13 purified from mycobacteria under normal growth conditions, captured with native substrates. Structures define the ketosynthase (KS), linker and acyl transferase (AT) domains at 1.8 A resolution and two alternative locations of the N-terminal acyl carrier protein. These structures suggest intermediate states on the pathway for substrate delivery to the KS domain. Other domains, visible at lower resolution, are flexible relative to the KS-AT core. The chemical structures of three bound endogenous long-chain fatty acid substrates were determined by electrospray ionization mass spectrometry.


Authors: Kim, S.K., Dickinson, M.S., Finer-Moore, J.S., Rosenberg, O.S., Stroud, R.M.
Structure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13.,Kim SK, Dickinson MS, Finer-Moore J, Guan Z, Kaake RM, Echeverria I, Chen J, Pulido EH, Sali A, Krogan NJ, Rosenberg OS, Stroud RM Nat Struct Mol Biol. 2023 Mar;30(3):296-308. doi: 10.1038/s41594-022-00918-0. , Epub 2023 Feb 13. PMID:36782050<ref>PMID:36782050</ref>


Description: ACP1-KS-AT domains of mycobacterial Pks13
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Rosenberg, O.S]]
<div class="pdbe-citations 8cv1" style="background-color:#fffaf0;"></div>
[[Category: Dickinson, M.S]]
== References ==
[[Category: Kim, S.K]]
<references/>
[[Category: Finer-Moore, J.S]]
__TOC__
[[Category: Stroud, R.M]]
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: Dickinson MS]]
[[Category: Finer-Moore JS]]
[[Category: Kim SK]]
[[Category: Rosenberg OS]]
[[Category: Stroud RM]]

Latest revision as of 10:07, 21 November 2024

ACP1-KS-AT domains of mycobacterial Pks13ACP1-KS-AT domains of mycobacterial Pks13

Structural highlights

8cv1 is a 2 chain structure with sequence from Mycolicibacterium smegmatis MC2 155. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

I7FMV0_MYCS2

Publication Abstract from PubMed

The mycolic acid layer of the Mycobacterium tuberculosis cell wall is essential for viability and virulence, and the enzymes responsible for its synthesis are targets for antimycobacterial drug development. Polyketide synthase 13 (Pks13) is a module encoding several enzymatic and transport functions that carries out the condensation of two different long-chain fatty acids to produce mycolic acids. We determined structures by cryogenic-electron microscopy of dimeric multi-enzyme Pks13 purified from mycobacteria under normal growth conditions, captured with native substrates. Structures define the ketosynthase (KS), linker and acyl transferase (AT) domains at 1.8 A resolution and two alternative locations of the N-terminal acyl carrier protein. These structures suggest intermediate states on the pathway for substrate delivery to the KS domain. Other domains, visible at lower resolution, are flexible relative to the KS-AT core. The chemical structures of three bound endogenous long-chain fatty acid substrates were determined by electrospray ionization mass spectrometry.

Structure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13.,Kim SK, Dickinson MS, Finer-Moore J, Guan Z, Kaake RM, Echeverria I, Chen J, Pulido EH, Sali A, Krogan NJ, Rosenberg OS, Stroud RM Nat Struct Mol Biol. 2023 Mar;30(3):296-308. doi: 10.1038/s41594-022-00918-0. , Epub 2023 Feb 13. PMID:36782050[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Kim SK, Dickinson MS, Finer-Moore J, Guan Z, Kaake RM, Echeverria I, Chen J, Pulido EH, Sali A, Krogan NJ, Rosenberg OS, Stroud RM. Structure and dynamics of the essential endogenous mycobacterial polyketide synthase Pks13. Nat Struct Mol Biol. 2023 Mar;30(3):296-308. PMID:36782050 doi:10.1038/s41594-022-00918-0

8cv1, resolution 2.60Å

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