7ax5: Difference between revisions
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New page: '''Unreleased structure''' The entry 7ax5 is ON HOLD until Paper Publication Authors: Dietl, A., Barends, T. Description: Anammox-specific acyl carrier protein from Kuenenia stuttgarti... |
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==Anammox-specific acyl carrier protein from Kuenenia stuttgartiensis; ensemble refinement== | |||
<StructureSection load='7ax5' size='340' side='right'caption='[[7ax5]], [[Resolution|resolution]] 1.76Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AX5 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]] 1.756Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7ax5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ax5 OCA], [https://pdbe.org/7ax5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ax5 RCSB], [https://www.ebi.ac.uk/pdbsum/7ax5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ax5 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Anaerobic ammonium-oxidizing (anammox) bacteria express a distinct acyl carrier protein implicated in the biosynthesis of the highly unusual "ladderane" lipids these organisms produce. This "anammox-specific" ACP, or amxACP, shows several unique features such as a conserved FF motif and an unusual sequence in the functionally important helix III. Investigation of the protein's structure and dynamics, both in the crystal by ensemble refinement and by MD simulations, reveals that helix III adopts a rare six-residue-long 310 -helical conformation that confers a large degree of conformational and positional variability on this part of the protein. This way of introducing structural flexibility by using the inherent properties of 310 -helices appears unique among ACPs. Moreover, the structure suggests a role for the FF motif in shielding the thioester linkage between the protein's prosthetic group and its acyl cargo from hydrolysis. | |||
Dynamics in an unusual acyl carrier protein from a ladderane lipid-synthesizing organism.,Dietl A, Barends TRM Proteins. 2021 Jul 26. doi: 10.1002/prot.26187. PMID:34310758<ref>PMID:34310758</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7ax5" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Barends T]] | |||
[[Category: Dietl A]] | |||
Latest revision as of 06:11, 19 June 2024
Anammox-specific acyl carrier protein from Kuenenia stuttgartiensis; ensemble refinement
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