6n3p: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (3 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Crosslinked AcpP=FabZ complex from E. coli Type II FAS== | |||
<StructureSection load='6n3p' size='340' side='right'caption='[[6n3p]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6n3p]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N3P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N3P 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]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=XLN:N~3~-{(2R)-4-[(dihydroxyphosphanyl)oxy]-2-hydroxy-3,3-dimethylbutanoyl}-N-(3-{[(1Z)-pent-1-en-1-yl]sulfonyl}propyl)-beta-alaninamide'>XLN</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=6n3p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n3p OCA], [https://pdbe.org/6n3p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n3p RCSB], [https://www.ebi.ac.uk/pdbsum/6n3p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n3p ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/FABZ_ECOLI FABZ_ECOLI] Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.<ref>PMID:10629181</ref> <ref>PMID:7806516</ref> <ref>PMID:8910376</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fatty acid biosynthesis in alpha- and gamma-proteobacteria requires two functionally distinct dehydratases, FabA and FabZ. Here, mechanistic cross-linking facilitates the structural characterization of a stable hexameric complex of six Escherichia coli FabZ dehydratase subunits with six AcpP acyl carrier proteins. The crystal structure sheds light on the divergent substrate selectivity of FabA and FabZ by revealing distinct architectures of the binding pocket. Molecular dynamics simulations demonstrate differential biasing of substrate orientations and conformations within the active sites of FabA and FabZ such that FabZ is preorganized to catalyze only dehydration, while FabA is primed for both dehydration and isomerization. | |||
Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli.,Dodge GJ, Patel A, Jaremko KL, McCammon JA, Smith JL, Burkart MD Proc Natl Acad Sci U S A. 2019 Mar 14. pii: 1818686116. doi:, 10.1073/pnas.1818686116. PMID:30872475<ref>PMID:30872475</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6n3p" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Acyl carrier protein 3D structures|Acyl carrier protein 3D structures]] | |||
*[[Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures|Beta-hydroxyacyl-acyl carrier protein dehydratase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Dodge GJ]] | |||
[[Category: Smith JL]] | |||
Latest revision as of 09:44, 11 October 2023
Crosslinked AcpP=FabZ complex from E. coli Type II FASCrosslinked AcpP=FabZ complex from E. coli Type II FAS
Structural highlights
FunctionFABZ_ECOLI Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs.[1] [2] [3] Publication Abstract from PubMedFatty acid biosynthesis in alpha- and gamma-proteobacteria requires two functionally distinct dehydratases, FabA and FabZ. Here, mechanistic cross-linking facilitates the structural characterization of a stable hexameric complex of six Escherichia coli FabZ dehydratase subunits with six AcpP acyl carrier proteins. The crystal structure sheds light on the divergent substrate selectivity of FabA and FabZ by revealing distinct architectures of the binding pocket. Molecular dynamics simulations demonstrate differential biasing of substrate orientations and conformations within the active sites of FabA and FabZ such that FabZ is preorganized to catalyze only dehydration, while FabA is primed for both dehydration and isomerization. Structural and dynamical rationale for fatty acid unsaturation in Escherichia coli.,Dodge GJ, Patel A, Jaremko KL, McCammon JA, Smith JL, Burkart MD Proc Natl Acad Sci U S A. 2019 Mar 14. pii: 1818686116. doi:, 10.1073/pnas.1818686116. PMID:30872475[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||